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PDBsum entry 3scr

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
3scr
Jmol
Contents
Protein chains
472 a.a.
Ligands
SO4 ×2
MES ×2
GOL ×2
Metals
_ZN
Waters ×865
HEADER    HYDROLASE                               08-JUN-11   3SCR
TITLE     CRYSTAL STRUCTURE OF RICE BGLU1 E386S MUTANT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BETA-GLUCOSIDASE 7;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: OS3BGLU7;
COMPND   5 EC: 3.2.1.21;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;
SOURCE   3 ORGANISM_COMMON: JAPANESE RICE;
SOURCE   4 ORGANISM_TAXID: 39947;
SOURCE   5 STRAIN: ORION;
SOURCE   6 GENE: BGLU1, BGLU7, LOC_OS03G49600, OS03G0703000, OS3BGLU7,
SOURCE   7 OSJNBA0004L11.16;
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: ORIGAMI(DE3);
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PET32A(+)
KEYWDS    BETA-ALPHA-BARRELS, GLYCOSYNTHASE, OLIGOSACCHARIDE SYNTHESIS,
KEYWDS   2 TRANSGLUCOSYLATION, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.PENGTHAISONG,S.G.WITHERS,B.KUAPRASERT,J.R.KETUDAT CAIRNS
REVDAT   1   13-JUN-12 3SCR    0
JRNL        AUTH   S.PENGTHAISONG,S.G.WITHERS,B.KUAPRASERT,J.R.KETUDAT CAIRNS
JRNL        TITL   STRUCTURAL INVESTIGATION OF THE BASIS FOR
JRNL        TITL 2 CELLOOLIGOSACCHARIDE SYNTHESIS BY RICE BGLU1 GLYCOSYNTHASES
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0110
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.76
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 90324
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178
REMARK   3   R VALUE            (WORKING SET) : 0.177
REMARK   3   FREE R VALUE                     : 0.208
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 4702
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6532
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.78
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300
REMARK   3   BIN FREE R VALUE SET COUNT          : 335
REMARK   3   BIN FREE R VALUE                    : 0.2930
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7612
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 47
REMARK   3   SOLVENT ATOMS            : 865
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.85
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.26000
REMARK   3    B22 (A**2) : 1.29000
REMARK   3    B33 (A**2) : -1.03000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.126
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.118
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.072
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.283
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7888 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10720 ; 1.397 ; 1.927
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   942 ; 5.987 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   400 ;34.106 ;23.650
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1204 ;12.669 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;21.044 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1082 ; 0.153 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6212 ; 0.006 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4684 ; 0.633 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7498 ; 1.180 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3204 ; 2.075 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3222 ; 3.312 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      5       A     476      4
REMARK   3           1     B      5       B     476      4
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3806 ;  0.06 ;  0.50
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3806 ;  0.51 ;  2.00
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3SCR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JUN-11.
REMARK 100 THE RCSB ID CODE IS RCSB066044.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-AUG-09
REMARK 200  TEMPERATURE           (KELVIN) : 105
REMARK 200  PH                             : 6.7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSRRC
REMARK 200  BEAMLINE                       : BL13B1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95127
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 7.200
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.11200
REMARK 200   FOR THE DATA SET  : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.46200
REMARK 200   FOR SHELL         : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC 5.5.0110
REMARK 200 STARTING MODEL: 2RGL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG MME 5000, 0.20M AMMONIUM
REMARK 280  SULFATE, 0.1M MES, PH 6.7, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 288.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       39.87000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.74650
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.48300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.74650
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.87000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.48300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ALA A    -4
REMARK 465     MET A    -3
REMARK 465     ALA A    -2
REMARK 465     ASP A    -1
REMARK 465     VAL A     0
REMARK 465     VAL A     1
REMARK 465     PRO A     2
REMARK 465     LYS A     3
REMARK 465     PRO A     4
REMARK 465     ALA B    -4
REMARK 465     MET B    -3
REMARK 465     ALA B    -2
REMARK 465     ASP B    -1
REMARK 465     VAL B     0
REMARK 465     VAL B     1
REMARK 465     PRO B     2
REMARK 465     LYS B     3
REMARK 465     PRO B     4
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ALA A  63     -130.12     52.26
REMARK 500    TYR A 131       -1.66     70.57
REMARK 500    ASP A 132       49.74   -108.30
REMARK 500    ASP A 186      -68.17   -100.61
REMARK 500    ASN A 203      103.34   -160.89
REMARK 500    LYS A 289     -123.64     56.62
REMARK 500    ALA A 354     -164.24    -77.30
REMARK 500    ASP A 403       58.91    -92.43
REMARK 500    TRP A 441     -121.98     49.75
REMARK 500    ALA B  63     -126.44     53.39
REMARK 500    TYR B 131       -3.51     72.54
REMARK 500    ASP B 132       49.31   -106.80
REMARK 500    ASP B 186      -64.72   -104.34
REMARK 500    ASN B 203      102.98   -162.90
REMARK 500    HIS B 267      -63.45    -91.74
REMARK 500    LYS B 289     -124.59     55.21
REMARK 500    ALA B 354     -163.09    -78.31
REMARK 500    TRP B 441     -124.36     50.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1001  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  68   ND1
REMARK 620 2 HIS B  68   ND1 119.7
REMARK 620 3 ASP B  65   OD2  99.1 120.4
REMARK 620 4 ASP A  65   OD2 120.3 101.2  94.6
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1008
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2RGL   RELATED DB: PDB
REMARK 900 RICE BGLU1 BETA-GLUCOSIDASE, A PLANT EXOGLUCANASE BETA-
REMARK 900 GLUCOSIDASE.
REMARK 900 RELATED ID: 2RGM   RELATED DB: PDB
REMARK 900 RICE BGLU1 BETA-GLUCOSIDASE COMPLEXED WITH 2-DEOXY-2-
REMARK 900 FLUOROGLUCOSIDE.
REMARK 900 RELATED ID: 3F4V   RELATED DB: PDB
REMARK 900 SEMI-ACTIVE E176Q MUTANT OF RICE BGLU1, A PLANT
REMARK 900 EXOGLUCANASE BETA-GLUCOSIDASE.
REMARK 900 RELATED ID: 3F5I   RELATED DB: PDB
REMARK 900 SEMI-ACTIVE E176Q MUTANT OF RICE BGLU1 COMPLEXED WITH 2-
REMARK 900 DEOXY-2-FLUOROGLUCOSIDE.
REMARK 900 RELATED ID: 3F5J   RELATED DB: PDB
REMARK 900 SEMI-ACTIVE E176Q MUTANT OF RICE BGLU1 COMPLEXED WITH
REMARK 900 CELLOTETRAOSE.
REMARK 900 RELATED ID: 3F5K   RELATED DB: PDB
REMARK 900 SEMI-ACTIVE E176Q MUTANT OF RICE BGLU1 COMPLEXED WITH
REMARK 900 CELLOPENTAOSE.
REMARK 900 RELATED ID: 3AHT   RELATED DB: PDB
REMARK 900 SEMI-ACTIVE E176Q MUTANT OF RICE BGLU1 COMPLEXED WITH
REMARK 900 LAMINARIBIOSE.
REMARK 900 RELATED ID: 3SCN   RELATED DB: PDB
REMARK 900 RELATED ID: 3SCO   RELATED DB: PDB
REMARK 900 RELATED ID: 3SCP   RELATED DB: PDB
REMARK 900 RELATED ID: 3SCQ   RELATED DB: PDB
REMARK 900 RELATED ID: 3SCS   RELATED DB: PDB
REMARK 900 RELATED ID: 3SCT   RELATED DB: PDB
REMARK 900 RELATED ID: 3SCU   RELATED DB: PDB
REMARK 900 RELATED ID: 3SCV   RELATED DB: PDB
REMARK 900 RELATED ID: 3SCW   RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS CONFLICT IS IN GENBANK DATABASE AAA84906.
DBREF  3SCR A    1   476  UNP    Q75I93   BGL07_ORYSJ     29    504
DBREF  3SCR B    1   476  UNP    Q75I93   BGL07_ORYSJ     29    504
SEQADV 3SCR ALA A   -4  UNP  Q75I93              EXPRESSION TAG
SEQADV 3SCR MET A   -3  UNP  Q75I93              EXPRESSION TAG
SEQADV 3SCR ALA A   -2  UNP  Q75I93              EXPRESSION TAG
SEQADV 3SCR ASP A   -1  UNP  Q75I93              EXPRESSION TAG
SEQADV 3SCR VAL A    0  UNP  Q75I93              EXPRESSION TAG
SEQADV 3SCR VAL A   24  UNP  Q75I93    ALA    52 SEE REMARK 999
SEQADV 3SCR SER A  386  UNP  Q75I93    GLU   414 ENGINEERED MUTATION
SEQADV 3SCR ALA B   -4  UNP  Q75I93              EXPRESSION TAG
SEQADV 3SCR MET B   -3  UNP  Q75I93              EXPRESSION TAG
SEQADV 3SCR ALA B   -2  UNP  Q75I93              EXPRESSION TAG
SEQADV 3SCR ASP B   -1  UNP  Q75I93              EXPRESSION TAG
SEQADV 3SCR VAL B    0  UNP  Q75I93              EXPRESSION TAG
SEQADV 3SCR VAL B   24  UNP  Q75I93    ALA    52 SEE REMARK 999
SEQADV 3SCR SER B  386  UNP  Q75I93    GLU   414 ENGINEERED MUTATION
SEQRES   1 A  481  ALA MET ALA ASP VAL VAL PRO LYS PRO ASN TRP LEU GLY
SEQRES   2 A  481  GLY LEU SER ARG ALA ALA PHE PRO LYS ARG PHE VAL PHE
SEQRES   3 A  481  GLY THR VAL THR SER ALA TYR GLN VAL GLU GLY MET ALA
SEQRES   4 A  481  ALA SER GLY GLY ARG GLY PRO SER ILE TRP ASP ALA PHE
SEQRES   5 A  481  ALA HIS THR PRO GLY ASN VAL ALA GLY ASN GLN ASN GLY
SEQRES   6 A  481  ASP VAL ALA THR ASP GLN TYR HIS ARG TYR LYS GLU ASP
SEQRES   7 A  481  VAL ASN LEU MET LYS SER LEU ASN PHE ASP ALA TYR ARG
SEQRES   8 A  481  PHE SER ILE SER TRP SER ARG ILE PHE PRO ASP GLY GLU
SEQRES   9 A  481  GLY ARG VAL ASN GLN GLU GLY VAL ALA TYR TYR ASN ASN
SEQRES  10 A  481  LEU ILE ASN TYR LEU LEU GLN LYS GLY ILE THR PRO TYR
SEQRES  11 A  481  VAL ASN LEU TYR HIS TYR ASP LEU PRO LEU ALA LEU GLU
SEQRES  12 A  481  LYS LYS TYR GLY GLY TRP LEU ASN ALA LYS MET ALA ASP
SEQRES  13 A  481  LEU PHE THR GLU TYR ALA ASP PHE CYS PHE LYS THR PHE
SEQRES  14 A  481  GLY ASN ARG VAL LYS HIS TRP PHE THR PHE ASN GLU PRO
SEQRES  15 A  481  ARG ILE VAL ALA LEU LEU GLY TYR ASP GLN GLY THR ASN
SEQRES  16 A  481  PRO PRO LYS ARG CYS THR LYS CYS ALA ALA GLY GLY ASN
SEQRES  17 A  481  SER ALA THR GLU PRO TYR ILE VAL ALA HIS ASN PHE LEU
SEQRES  18 A  481  LEU SER HIS ALA ALA ALA VAL ALA ARG TYR ARG THR LYS
SEQRES  19 A  481  TYR GLN ALA ALA GLN GLN GLY LYS VAL GLY ILE VAL LEU
SEQRES  20 A  481  ASP PHE ASN TRP TYR GLU ALA LEU SER ASN SER THR GLU
SEQRES  21 A  481  ASP GLN ALA ALA ALA GLN ARG ALA ARG ASP PHE HIS ILE
SEQRES  22 A  481  GLY TRP TYR LEU ASP PRO LEU ILE ASN GLY HIS TYR PRO
SEQRES  23 A  481  GLN ILE MET GLN ASP LEU VAL LYS ASP ARG LEU PRO LYS
SEQRES  24 A  481  PHE THR PRO GLU GLN ALA ARG LEU VAL LYS GLY SER ALA
SEQRES  25 A  481  ASP TYR ILE GLY ILE ASN GLN TYR THR ALA SER TYR MET
SEQRES  26 A  481  LYS GLY GLN GLN LEU MET GLN GLN THR PRO THR SER TYR
SEQRES  27 A  481  SER ALA ASP TRP GLN VAL THR TYR VAL PHE ALA LYS ASN
SEQRES  28 A  481  GLY LYS PRO ILE GLY PRO GLN ALA ASN SER ASN TRP LEU
SEQRES  29 A  481  TYR ILE VAL PRO TRP GLY MET TYR GLY CYS VAL ASN TYR
SEQRES  30 A  481  ILE LYS GLN LYS TYR GLY ASN PRO THR VAL VAL ILE THR
SEQRES  31 A  481  SER ASN GLY MET ASP GLN PRO ALA ASN LEU SER ARG ASP
SEQRES  32 A  481  GLN TYR LEU ARG ASP THR THR ARG VAL HIS PHE TYR ARG
SEQRES  33 A  481  SER TYR LEU THR GLN LEU LYS LYS ALA ILE ASP GLU GLY
SEQRES  34 A  481  ALA ASN VAL ALA GLY TYR PHE ALA TRP SER LEU LEU ASP
SEQRES  35 A  481  ASN PHE GLU TRP LEU SER GLY TYR THR SER LYS PHE GLY
SEQRES  36 A  481  ILE VAL TYR VAL ASP PHE ASN THR LEU GLU ARG HIS PRO
SEQRES  37 A  481  LYS ALA SER ALA TYR TRP PHE ARG ASP MET LEU LYS HIS
SEQRES   1 B  481  ALA MET ALA ASP VAL VAL PRO LYS PRO ASN TRP LEU GLY
SEQRES   2 B  481  GLY LEU SER ARG ALA ALA PHE PRO LYS ARG PHE VAL PHE
SEQRES   3 B  481  GLY THR VAL THR SER ALA TYR GLN VAL GLU GLY MET ALA
SEQRES   4 B  481  ALA SER GLY GLY ARG GLY PRO SER ILE TRP ASP ALA PHE
SEQRES   5 B  481  ALA HIS THR PRO GLY ASN VAL ALA GLY ASN GLN ASN GLY
SEQRES   6 B  481  ASP VAL ALA THR ASP GLN TYR HIS ARG TYR LYS GLU ASP
SEQRES   7 B  481  VAL ASN LEU MET LYS SER LEU ASN PHE ASP ALA TYR ARG
SEQRES   8 B  481  PHE SER ILE SER TRP SER ARG ILE PHE PRO ASP GLY GLU
SEQRES   9 B  481  GLY ARG VAL ASN GLN GLU GLY VAL ALA TYR TYR ASN ASN
SEQRES  10 B  481  LEU ILE ASN TYR LEU LEU GLN LYS GLY ILE THR PRO TYR
SEQRES  11 B  481  VAL ASN LEU TYR HIS TYR ASP LEU PRO LEU ALA LEU GLU
SEQRES  12 B  481  LYS LYS TYR GLY GLY TRP LEU ASN ALA LYS MET ALA ASP
SEQRES  13 B  481  LEU PHE THR GLU TYR ALA ASP PHE CYS PHE LYS THR PHE
SEQRES  14 B  481  GLY ASN ARG VAL LYS HIS TRP PHE THR PHE ASN GLU PRO
SEQRES  15 B  481  ARG ILE VAL ALA LEU LEU GLY TYR ASP GLN GLY THR ASN
SEQRES  16 B  481  PRO PRO LYS ARG CYS THR LYS CYS ALA ALA GLY GLY ASN
SEQRES  17 B  481  SER ALA THR GLU PRO TYR ILE VAL ALA HIS ASN PHE LEU
SEQRES  18 B  481  LEU SER HIS ALA ALA ALA VAL ALA ARG TYR ARG THR LYS
SEQRES  19 B  481  TYR GLN ALA ALA GLN GLN GLY LYS VAL GLY ILE VAL LEU
SEQRES  20 B  481  ASP PHE ASN TRP TYR GLU ALA LEU SER ASN SER THR GLU
SEQRES  21 B  481  ASP GLN ALA ALA ALA GLN ARG ALA ARG ASP PHE HIS ILE
SEQRES  22 B  481  GLY TRP TYR LEU ASP PRO LEU ILE ASN GLY HIS TYR PRO
SEQRES  23 B  481  GLN ILE MET GLN ASP LEU VAL LYS ASP ARG LEU PRO LYS
SEQRES  24 B  481  PHE THR PRO GLU GLN ALA ARG LEU VAL LYS GLY SER ALA
SEQRES  25 B  481  ASP TYR ILE GLY ILE ASN GLN TYR THR ALA SER TYR MET
SEQRES  26 B  481  LYS GLY GLN GLN LEU MET GLN GLN THR PRO THR SER TYR
SEQRES  27 B  481  SER ALA ASP TRP GLN VAL THR TYR VAL PHE ALA LYS ASN
SEQRES  28 B  481  GLY LYS PRO ILE GLY PRO GLN ALA ASN SER ASN TRP LEU
SEQRES  29 B  481  TYR ILE VAL PRO TRP GLY MET TYR GLY CYS VAL ASN TYR
SEQRES  30 B  481  ILE LYS GLN LYS TYR GLY ASN PRO THR VAL VAL ILE THR
SEQRES  31 B  481  SER ASN GLY MET ASP GLN PRO ALA ASN LEU SER ARG ASP
SEQRES  32 B  481  GLN TYR LEU ARG ASP THR THR ARG VAL HIS PHE TYR ARG
SEQRES  33 B  481  SER TYR LEU THR GLN LEU LYS LYS ALA ILE ASP GLU GLY
SEQRES  34 B  481  ALA ASN VAL ALA GLY TYR PHE ALA TRP SER LEU LEU ASP
SEQRES  35 B  481  ASN PHE GLU TRP LEU SER GLY TYR THR SER LYS PHE GLY
SEQRES  36 B  481  ILE VAL TYR VAL ASP PHE ASN THR LEU GLU ARG HIS PRO
SEQRES  37 B  481  LYS ALA SER ALA TYR TRP PHE ARG ASP MET LEU LYS HIS
HET     ZN  A1001       1
HET    SO4  A1003       5
HET    MES  A1005      12
HET    GOL  A1007       6
HET    SO4  B1004       5
HET    MES  B1006      12
HET    GOL  B1008       6
HETNAM      ZN ZINC ION
HETNAM     SO4 SULFATE ION
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3   ZN    ZN 2+
FORMUL   4  SO4    2(O4 S 2-)
FORMUL   5  MES    2(C6 H13 N O4 S)
FORMUL   6  GOL    2(C3 H8 O3)
FORMUL  10  HOH   *865(H2 O)
HELIX    1   1 SER A   11  PHE A   15  5                                   5
HELIX    2   2 SER A   26  GLU A   31  1                                   6
HELIX    3   3 SER A   42  HIS A   49  1                                   8
HELIX    4   4 VAL A   54  GLN A   58  5                                   5
HELIX    5   5 ASP A   65  LEU A   80  1                                  16
HELIX    6   6 SER A   90  PHE A   95  1                                   6
HELIX    7   7 ASN A  103  LYS A  120  1                                  18
HELIX    8   8 PRO A  134  GLY A  142  1                                   9
HELIX    9   9 GLY A  143  ALA A  147  5                                   5
HELIX   10  10 LYS A  148  GLY A  165  1                                  18
HELIX   11  11 GLU A  176  ASP A  186  1                                  11
HELIX   12  12 THR A  206  TYR A  230  1                                  25
HELIX   13  13 TYR A  230  GLN A  235  1                                   6
HELIX   14  14 SER A  253  ILE A  268  1                                  16
HELIX   15  15 ILE A  268  GLY A  278  1                                  11
HELIX   16  16 PRO A  281  LYS A  289  1                                   9
HELIX   17  17 ASP A  290  LEU A  292  5                                   3
HELIX   18  18 THR A  296  LYS A  304  1                                   9
HELIX   19  19 SER A  332  TRP A  337  1                                   6
HELIX   20  20 VAL A  362  TYR A  377  1                                  16
HELIX   21  21 SER A  396  ARG A  402  1                                   7
HELIX   22  22 ASP A  403  GLU A  423  1                                  21
HELIX   23  23 GLU A  440  TYR A  445  5                                   6
HELIX   24  24 LYS A  464  LEU A  474  1                                  11
HELIX   25  25 SER B   11  PHE B   15  5                                   5
HELIX   26  26 SER B   26  GLU B   31  1                                   6
HELIX   27  27 SER B   42  HIS B   49  1                                   8
HELIX   28  28 VAL B   54  GLN B   58  5                                   5
HELIX   29  29 ASP B   65  LEU B   80  1                                  16
HELIX   30  30 SER B   90  PHE B   95  1                                   6
HELIX   31  31 ASN B  103  LYS B  120  1                                  18
HELIX   32  32 PRO B  134  GLY B  142  1                                   9
HELIX   33  33 GLY B  143  ALA B  147  5                                   5
HELIX   34  34 LYS B  148  GLY B  165  1                                  18
HELIX   35  35 GLU B  176  ASP B  186  1                                  11
HELIX   36  36 THR B  206  TYR B  230  1                                  25
HELIX   37  37 TYR B  230  GLN B  235  1                                   6
HELIX   38  38 SER B  253  ILE B  268  1                                  16
HELIX   39  39 ILE B  268  GLY B  278  1                                  11
HELIX   40  40 PRO B  281  LYS B  289  1                                   9
HELIX   41  41 ASP B  290  LEU B  292  5                                   3
HELIX   42  42 THR B  296  LYS B  304  1                                   9
HELIX   43  43 SER B  334  GLN B  338  5                                   5
HELIX   44  44 VAL B  362  TYR B  377  1                                  16
HELIX   45  45 SER B  396  ARG B  402  1                                   7
HELIX   46  46 ASP B  403  GLU B  423  1                                  21
HELIX   47  47 GLU B  440  SER B  447  5                                   8
HELIX   48  48 LYS B  464  LYS B  475  1                                  12
SHEET    1   A 9 VAL A  20  VAL A  24  0
SHEET    2   A 9 ALA A  84  SER A  88  1  O  ARG A  86   N  THR A  23
SHEET    3   A 9 THR A 123  ASN A 127  1  O  TYR A 125   N  TYR A  85
SHEET    4   A 9 HIS A 170  ASN A 175  1  O  PHE A 172   N  VAL A 126
SHEET    5   A 9 LYS A 237  ASP A 243  1  O  GLY A 239   N  TRP A 171
SHEET    6   A 9 ILE A 310  ASN A 313  1  O  GLY A 311   N  ILE A 240
SHEET    7   A 9 VAL A 382  SER A 386  1  O  VAL A 383   N  ILE A 312
SHEET    8   A 9 VAL A 427  TRP A 433  1  O  ALA A 428   N  VAL A 382
SHEET    9   A 9 VAL A  20  VAL A  24  1  N  VAL A  20   O  TYR A 430
SHEET    1   B 3 TRP A 246  ALA A 249  0
SHEET    2   B 3 ALA A 317  LYS A 321  1  O  SER A 318   N  GLU A 248
SHEET    3   B 3 THR A 340  VAL A 342 -1  O  THR A 340   N  LYS A 321
SHEET    1   C 2 ALA A 344  LYS A 345  0
SHEET    2   C 2 LYS A 348  PRO A 349 -1  O  LYS A 348   N  LYS A 345
SHEET    1   D 2 GLN A 391  PRO A 392  0
SHEET    2   D 2 SER A 447  LYS A 448 -1  O  LYS A 448   N  GLN A 391
SHEET    1   E 2 VAL A 452  VAL A 454  0
SHEET    2   E 2 ARG A 461  PRO A 463 -1  O  HIS A 462   N  TYR A 453
SHEET    1   F 9 VAL B  20  VAL B  24  0
SHEET    2   F 9 ALA B  84  SER B  88  1  O  ARG B  86   N  THR B  23
SHEET    3   F 9 THR B 123  ASN B 127  1  O  TYR B 125   N  TYR B  85
SHEET    4   F 9 HIS B 170  ASN B 175  1  O  HIS B 170   N  VAL B 126
SHEET    5   F 9 LYS B 237  ASP B 243  1  O  LYS B 237   N  TRP B 171
SHEET    6   F 9 ILE B 310  ASN B 313  1  O  GLY B 311   N  LEU B 242
SHEET    7   F 9 VAL B 382  SER B 386  1  O  VAL B 383   N  ILE B 310
SHEET    8   F 9 VAL B 427  TRP B 433  1  O  ALA B 428   N  VAL B 382
SHEET    9   F 9 VAL B  20  VAL B  24  1  N  GLY B  22   O  TYR B 430
SHEET    1   G 3 TRP B 246  ALA B 249  0
SHEET    2   G 3 ALA B 317  LYS B 321  1  O  SER B 318   N  GLU B 248
SHEET    3   G 3 THR B 340  VAL B 342 -1  O  THR B 340   N  LYS B 321
SHEET    1   H 2 ALA B 344  LYS B 345  0
SHEET    2   H 2 LYS B 348  PRO B 349 -1  O  LYS B 348   N  LYS B 345
SHEET    1   I 2 VAL B 452  VAL B 454  0
SHEET    2   I 2 ARG B 461  PRO B 463 -1  O  HIS B 462   N  TYR B 453
SSBOND   1 CYS A  195    CYS A  198                          1555   1555  2.04
SSBOND   2 CYS B  195    CYS B  198                          1555   1555  2.04
LINK         ND1 HIS A  68                ZN    ZN A1001     1555   1555  1.99
LINK         ND1 HIS B  68                ZN    ZN A1001     1555   1555  2.00
LINK         OD2 ASP B  65                ZN    ZN A1001     1555   1555  2.02
LINK         OD2 ASP A  65                ZN    ZN A1001     1555   1555  2.05
CISPEP   1 PRO A  191    PRO A  192          0         5.09
CISPEP   2 TRP A  433    SER A  434          0         1.31
CISPEP   3 PRO B  191    PRO B  192          0         3.34
CISPEP   4 TRP B  433    SER B  434          0         2.95
SITE     1 AC1  4 ASP A  65  HIS A  68  ASP B  65  HIS B  68
SITE     1 AC2  5 THR A 163  ASN A 166  ARG A 167  HOH A 543
SITE     2 AC2  5 HOH A 547
SITE     1 AC3  9 GLY A 278  HIS A 279  TYR A 280  GLN A 285
SITE     2 AC3  9 LYS A 294  PHE A 295  ALA A 300  HOH A 688
SITE     3 AC3  9 HOH A 785
SITE     1 AC4  6 GLN A  29  HIS A 130  TRP A 433  GLU A 440
SITE     2 AC4  6 TRP A 441  HOH A 788
SITE     1 AC5  5 THR B 163  ASN B 166  ARG B 167  HOH B 554
SITE     2 AC5  5 HOH B 675
SITE     1 AC6 10 LEU A 395  GLY B 278  HIS B 279  TYR B 280
SITE     2 AC6 10 GLN B 285  LYS B 294  PHE B 295  ALA B 300
SITE     3 AC6 10 HOH B 762  HOH B 824
SITE     1 AC7  6 GLN B  29  HIS B 130  TRP B 433  GLU B 440
SITE     2 AC7  6 TRP B 441  HOH B 867
CRYST1   79.740  100.966  127.493  90.00  90.00  90.00 P 21 21 21    8
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.012541  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009904  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007844        0.00000
      
PROCHECK
Go to PROCHECK summary
 References