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PDBsum entry 3mna

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Lyase/lyase inhibitor PDB id
3mna
Jmol
Contents
Protein chain
257 a.a.
Ligands
DWH
GOL
Metals
_ZN
Waters ×340
HEADER    LYASE/LYASE INHIBITOR                   21-APR-10   3MNA
TITLE     THE CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH A
TITLE    2 1,3,5-TRIAZINE-SUBSTITUTED BENZENESULFONAMIDE INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE II, CA-II, CARBONATE DEHYDRATASE II,
COMPND   5 CARBONIC ANHYDRASE C, CAC;
COMPND   6 EC: 4.2.1.1;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CA2, HCA2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS    ZINC METALLOENZYME, INHIBITOR, SULFONAMIDE, LYASE, TRIAZINE, LYASE-
KEYWDS   2 LYASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.S.AVVARU,J.WAGNER,A.H.ROBBINS,R.MCKENNA
REVDAT   2   22-JUN-11 3MNA    1       JRNL
REVDAT   1   20-APR-11 3MNA    0
JRNL        AUTH   F.CARTA,V.GARAJ,A.MARESCA,J.WAGNER,B.S.AVVARU,A.H.ROBBINS,
JRNL        AUTH 2 A.SCOZZAFAVA,R.MCKENNA,C.T.SUPURAN
JRNL        TITL   SULFONAMIDES INCORPORATING 1,3,5-TRIAZINE MOIETIES
JRNL        TITL 2 SELECTIVELY AND POTENTLY INHIBIT CARBONIC ANHYDRASE
JRNL        TITL 3 TRANSMEMBRANE ISOFORMS IX, XII AND XIV OVER CYTOSOLIC
JRNL        TITL 4 ISOFORMS I AND II: SOLUTION AND X-RAY CRYSTALLOGRAPHIC
JRNL        TITL 5 STUDIES.
JRNL        REF    BIOORG.MED.CHEM.              V.  19  3105 2011
JRNL        REFN                   ISSN 0968-0896
JRNL        PMID   21515057
JRNL        DOI    10.1016/J.BMC.2011.04.005
REMARK   2
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.1_348)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.30
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.160
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4
REMARK   3   NUMBER OF REFLECTIONS             : 38719
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.147
REMARK   3   R VALUE            (WORKING SET) : 0.145
REMARK   3   FREE R VALUE                     : 0.169
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010
REMARK   3   FREE R VALUE TEST SET COUNT      : 1941
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 25.3350 -  3.6100    0.99     2714   150  0.1460 0.1620
REMARK   3     2  3.6100 -  2.8670    1.00     2672   135  0.1310 0.1510
REMARK   3     3  2.8670 -  2.5050    1.00     2628   154  0.1330 0.1580
REMARK   3     4  2.5050 -  2.2760    1.00     2640   144  0.1270 0.1500
REMARK   3     5  2.2760 -  2.1130    1.00     2622   125  0.1210 0.1430
REMARK   3     6  2.1130 -  1.9880    0.99     2645   144  0.1150 0.1390
REMARK   3     7  1.9880 -  1.8890    1.00     2636   116  0.1150 0.1530
REMARK   3     8  1.8890 -  1.8060    1.00     2592   145  0.1260 0.1480
REMARK   3     9  1.8060 -  1.7370    0.99     2614   149  0.1250 0.1570
REMARK   3    10  1.7370 -  1.6770    0.99     2616   139  0.1360 0.1640
REMARK   3    11  1.6770 -  1.6250    0.99     2598   135  0.1460 0.1970
REMARK   3    12  1.6250 -  1.5780    1.00     2638   127  0.1520 0.1890
REMARK   3    13  1.5780 -  1.5370    1.00     2578   145  0.1710 0.1940
REMARK   3    14  1.5370 -  1.4990    0.97     2585   133  0.1890 0.2200
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : 0.45
REMARK   3   B_SOL              : 44.35
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 23.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.66
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.08500
REMARK   3    B22 (A**2) : -1.56000
REMARK   3    B33 (A**2) : 1.64500
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 1.05800
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.009           2179
REMARK   3   ANGLE     :  1.344           2968
REMARK   3   CHIRALITY :  0.078            306
REMARK   3   PLANARITY :  0.006            385
REMARK   3   DIHEDRAL  : 14.242            814
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 2
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: chain A and not element H
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6525  -1.3919  15.9349
REMARK   3    T TENSOR
REMARK   3      T11:   0.0712 T22:   0.0653
REMARK   3      T33:   0.0871 T12:  -0.0026
REMARK   3      T13:   0.0067 T23:   0.0008
REMARK   3    L TENSOR
REMARK   3      L11:   0.4201 L22:   0.2549
REMARK   3      L33:   0.5166 L12:  -0.0947
REMARK   3      L13:   0.0366 L23:  -0.0128
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0059 S12:  -0.0390 S13:   0.0093
REMARK   3      S21:  -0.0215 S22:   0.0058 S23:   0.0053
REMARK   3      S31:   0.0088 S32:   0.0009 S33:  -0.0012
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: chain I and not element H
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3334   5.5716  13.0615
REMARK   3    T TENSOR
REMARK   3      T11:   0.1029 T22:   0.1041
REMARK   3      T33:   0.1259 T12:  -0.0135
REMARK   3      T13:   0.0170 T23:   0.0048
REMARK   3    L TENSOR
REMARK   3      L11:   0.4228 L22:   0.0742
REMARK   3      L33:   0.2640 L12:   0.1597
REMARK   3      L13:  -0.3317 L23:  -0.1323
REMARK   3    S TENSOR
REMARK   3      S11:   0.0271 S12:   0.0161 S13:   0.0755
REMARK   3      S21:  -0.0164 S22:   0.0042 S23:   0.0997
REMARK   3      S31:  -0.0116 S32:   0.0530 S33:  -0.0307
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3MNA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-10.
REMARK 100 THE RCSB ID CODE IS RCSB058758.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-10
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : RIGAKU VARIMAX
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38719
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.300
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 4.000
REMARK 200  R MERGE                    (I) : 0.07100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.31600
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.6.1_348
REMARK 200 STARTING MODEL: 2ILI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3M SODIUM CITRATE, 100MM TRIS-HCL,
REMARK 280  PH 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       20.61500
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 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     MET A     1
REMARK 465     SER A     2
REMARK 465     HIS A     3
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   HD1  HIS A    15     HZ1  LYS A    18              1.27
REMARK 500   HE2  HIS A   107     HH   TYR A   194              1.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500  HD22  ASN A   178     HZ2  LYS A   225     2455     1.53
REMARK 500  HE21  GLN A   158    HD21  ASN A   178     2445     1.58
REMARK 500
REMARK 500 REMARK: NULL
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    ARG A  27       56.84   -142.83
REMARK 500    ALA A  65     -169.03   -165.10
REMARK 500    LYS A 111       -1.86     72.49
REMARK 500    PHE A 176       70.21   -150.54
REMARK 500    ASN A 244       47.37    -94.18
REMARK 500    LYS A 252     -136.90     54.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 276        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH A 312        DISTANCE =  5.95 ANGSTROMS
REMARK 525    HOH A 468        DISTANCE =  5.01 ANGSTROMS
REMARK 525    HOH A 546        DISTANCE =  6.60 ANGSTROMS
REMARK 525    HOH A 585        DISTANCE =  5.31 ANGSTROMS
REMARK 525    HOH A 588        DISTANCE =  6.28 ANGSTROMS
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 A 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DWH A 263   N1
REMARK 620 2 HIS A  94   NE2 111.3
REMARK 620 3 HIS A  96   NE2 112.9 103.2
REMARK 620 4 HIS A 119   ND1 117.1 111.4  99.6
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 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DWH A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MMF   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH A SLIGHTLY DIFFERENT
REMARK 900 INHIBITOR
DBREF  3MNA A    1   261  UNP    P00918   CAH2_HUMAN       1    260
SEQRES   1 A  260  MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES   2 A  260  GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES   3 A  260  ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES   4 A  260  TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES   5 A  260  GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES   6 A  260  PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES   7 A  260  LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES   8 A  260  GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES   9 A  260  SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES  10 A  260  LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES  11 A  260  GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES  12 A  260  GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES  13 A  260  GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES  14 A  260  GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES  15 A  260  LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES  16 A  260  SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES  17 A  260  ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES  18 A  260  VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES  19 A  260  GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES  20 A  260  GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A 262       1
HET    DWH  A 263      36
HET    GOL  A 401      10
HETNAM      ZN ZINC ION
HETNAM     DWH METHYL N-{4-CHLORO-6-[(4-SULFAMOYLPHENYL)AMINO]-1,3,5-
HETNAM   2 DWH  TRIAZIN-2-YL}GLYCINATE
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2   ZN    ZN 2+
FORMUL   3  DWH    C12 H13 CL N6 O4 S
FORMUL   4  GOL    C3 H8 O3
FORMUL   5  HOH   *340(H2 O)
HELIX    1   1 HIS A   15  ASP A   19  5                                   5
HELIX    2   2 PHE A   20  GLY A   25  5                                   6
HELIX    3   3 LYS A  127  GLY A  129  5                                   3
HELIX    4   4 ASP A  130  VAL A  135  1                                   6
HELIX    5   5 LYS A  154  GLY A  156  5                                   3
HELIX    6   6 LEU A  157  LEU A  164  1                                   8
HELIX    7   7 ASP A  165  LYS A  168  5                                   4
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  ARG A  227  1                                   9
SHEET    1   A 2 ASP A  32  ILE A  33  0
SHEET    2   A 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33
SHEET    1   B10 LYS A  39  TYR A  40  0
SHEET    2   B10 LYS A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   B10 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4   B10 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B10 LEU A 141  VAL A 150  1  N  GLY A 145   O  ILE A 210
SHEET    6   B10 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 146
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  HIS A  94   O  HIS A 119
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9   B10 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   10   B10 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 LEU A  47  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  81 -1  O  VAL A  78   N  SER A  50
SHEET    3   C 6 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79
SHEET    4   C 6 ALA A 116  ASN A 124 -1  O  HIS A 119   N  HIS A  94
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  ILE A 146   N  LEU A 118
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  PHE A 147
LINK        ZN    ZN A 262                 N1  DWH A 263     1555   1555  1.95
LINK         NE2 HIS A  94                ZN    ZN A 262     1555   1555  2.01
LINK         NE2 HIS A  96                ZN    ZN A 262     1555   1555  2.04
LINK         ND1 HIS A 119                ZN    ZN A 262     1555   1555  2.04
CISPEP   1 SER A   29    PRO A   30          0        -0.21
CISPEP   2 PRO A  201    PRO A  202          0         6.43
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  DWH A 263
SITE     1 AC2 16 GLN A  92  HIS A  94  HIS A  96  HIS A 119
SITE     2 AC2 16 PHE A 131  LEU A 198  THR A 199  THR A 200
SITE     3 AC2 16 TRP A 209   ZN A 262  HOH A 313  HOH A 330
SITE     4 AC2 16 GOL A 401  HOH A 467  HOH A 485  HOH A 502
SITE     1 AC3 10 ASN A  62  HIS A  64  ALA A  65  ASN A  67
SITE     2 AC3 10 GLN A  92  HIS A  94  DWH A 263  HOH A 350
SITE     3 AC3 10 HOH A 356  HOH A 502
CRYST1   42.360   41.230   72.023  90.00 104.24  90.00 P 1 21 1      2
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      0.023607  0.000000  0.005993        0.00000
SCALE2      0.000000  0.024254  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014325        0.00000
      
PROCHECK
Go to PROCHECK summary
 References