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PDBsum entry 1o8a

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Metalloprotease PDB id
1o8a
Jmol
Contents
Protein chain
575 a.a. *
Ligands
NAG ×5
NDG
ACT
NXA
Metals
_CL ×2
_ZN
Waters ×504
* Residue conservation analysis
HEADER    METALLOPROTEASE                         26-NOV-02   1O8A
TITLE     CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERTING ENZYME
TITLE    2 (NATIVE).
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ANGIOTENSIN CONVERTING ENZYME;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 68-656;
COMPND   5 SYNONYM: ACE-T, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II;
COMPND   6 EC: 3.4.15.1;
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 ORGAN: TESTIS;
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS    METALLOPROTEASE, ACE, PEPTIDYL DIPEPTIDASE, TYPE-I
KEYWDS   2 MEMBRANE-ANCHORED PROTEIN.
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.NATESH,S.L.U.SCHWAGER,E.D.STURROCK,K.R.ACHARYA
REVDAT   4   24-FEB-09 1O8A    1       VERSN
REVDAT   3   06-MAR-06 1O8A    1       TITLE  REMARK
REVDAT   2   11-JUL-03 1O8A    1       JRNL
REVDAT   1   07-FEB-03 1O8A    0
JRNL        AUTH   R.NATESH,S.L.U.SCHWAGER,E.D.STURROCK,K.R.ACHARYA
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN
JRNL        TITL 2 ANGIOTENSIN-CONVERTING ENZYME-LISINOPRIL COMPLEX
JRNL        REF    NATURE                        V. 421   551 2003
JRNL        REFN                   ISSN 0028-0836
JRNL        PMID   12540854
JRNL        DOI    10.1038/NATURE01370
REMARK   2
REMARK   2 RESOLUTION.    2.0  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.0
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.14
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.1
REMARK   3   NUMBER OF REFLECTIONS             : 41402
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 SET) : 0.18
REMARK   3   FREE R VALUE                     : 0.22
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.8
REMARK   3   FREE R VALUE TEST SET COUNT      : 1675
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4660
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 100
REMARK   3   SOLVENT ATOMS            : 504
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 23.9
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.4
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.29
REMARK   3   ESD FROM SIGMAA              (A) : 0.19
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.0
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.31
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.20
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.22
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.35
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.81
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : ION.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1O8A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-NOV-02.
REMARK 100 THE PDBE ID CODE IS EBI-11783.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-02
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 4.70
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SRS
REMARK 200  BEAMLINE                       : PX14.1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488
REMARK 200  MONOCHROMATOR                  : SI
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42782
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8
REMARK 200  DATA REDUNDANCY                : 7.100
REMARK 200  R MERGE                    (I) : 0.08100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 22.4600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.43200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.440
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1O86
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): 49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000/SODIUM ACETATE.
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       28.31000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.89500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.53000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.89500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.31000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.53000
REMARK 290   SMTRY3   4  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 GENERATING THE BIOMOLECULE
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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400  CONVERTS ANGIOTENSIN I TO ANGIOTENSIN II BY RELEASE OF
REMARK 400  THE TERMINAL HIS-LEU, THIS RESULTS IN AN INCREASE OF THE
REMARK 400  VASOCONSTRICTOR ACTIVITY OF ANGIOTENSIN. ALSO ABLE TO INACTIVATE
REMARK 400  BRADYKININ, A POTENT VASODILATOR  AND ACTS ON VARIOUS OTHER
REMARK 400  OLIGOPEPTIDES WITH FREE C-TERMINUS.
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     LEU A    37
REMARK 465     VAL A    38
REMARK 465     THR A    39
REMARK 465     SER A   435
REMARK 465     GLU A   436
REMARK 465     GLY A   437
REMARK 465     GLY A   438
REMARK 465     TYR A   619
REMARK 465     ASN A   620
REMARK 465     TRP A   621
REMARK 465     THR A   622
REMARK 465     PRO A   623
REMARK 465     ASN A   624
REMARK 465     SER A   625
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ASP A  40    CG   OD1  OD2
REMARK 470     GLU A  64    CG   CD   OE1  OE2
REMARK 470     LYS A 117    CG   CD   CE   NZ
REMARK 470     SER A 298    OG
REMARK 470     GLU A 303    CG   CD   OE1  OE2
REMARK 470     LYS A 307    CG   CD   CE   NZ
REMARK 470     SER A 439    CB   OG
REMARK 470     ASP A 440    CG   OD1  OD2
REMARK 470     GLN A 618    CA   C    O    CB   CG   CD   OE1  NE2
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 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    ASN A  72       76.67   -169.41
REMARK 500    GLU A 123     -136.53     49.77
REMARK 500    LYS A 363      -39.81   -133.03
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 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 701  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 383   NE2
REMARK 620 2 HIS A 387   NE2 106.6
REMARK 620 3 GLU A 411   OE1  95.6 105.0
REMARK 620 4 ACT A 700   O   101.8  89.5 153.1
REMARK 620 5 ACT A 700   OXT 118.9 127.5  95.5  58.2
REMARK 620 N                    1     2     3     4
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 691
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 692
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 693
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 694
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 696
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 695
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NXA A 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1O86   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN
REMARK 900  CONVERTING ENZYME IN COMPLEX WITH LISINOPRIL.
DBREF  1O8A A   37   625  UNP    P22966   ACET_HUMAN      68    656
SEQRES   1 A  589  LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL GLU
SEQRES   2 A  589  GLU TYR ASP ARG THR SER GLN VAL VAL TRP ASN GLU TYR
SEQRES   3 A  589  ALA GLU ALA ASN TRP ASN TYR ASN THR ASN ILE THR THR
SEQRES   4 A  589  GLU THR SER LYS ILE LEU LEU GLN LYS ASN MET GLN ILE
SEQRES   5 A  589  ALA ASN HIS THR LEU LYS TYR GLY THR GLN ALA ARG LYS
SEQRES   6 A  589  PHE ASP VAL ASN GLN LEU GLN ASN THR THR ILE LYS ARG
SEQRES   7 A  589  ILE ILE LYS LYS VAL GLN ASP LEU GLU ARG ALA ALA LEU
SEQRES   8 A  589  PRO ALA GLN GLU LEU GLU GLU TYR ASN LYS ILE LEU LEU
SEQRES   9 A  589  ASP MET GLU THR THR TYR SER VAL ALA THR VAL CYS HIS
SEQRES  10 A  589  PRO ASN GLY SER CYS LEU GLN LEU GLU PRO ASP LEU THR
SEQRES  11 A  589  ASN VAL MET ALA THR SER ARG LYS TYR GLU ASP LEU LEU
SEQRES  12 A  589  TRP ALA TRP GLU GLY TRP ARG ASP LYS ALA GLY ARG ALA
SEQRES  13 A  589  ILE LEU GLN PHE TYR PRO LYS TYR VAL GLU LEU ILE ASN
SEQRES  14 A  589  GLN ALA ALA ARG LEU ASN GLY TYR VAL ASP ALA GLY ASP
SEQRES  15 A  589  SER TRP ARG SER MET TYR GLU THR PRO SER LEU GLU GLN
SEQRES  16 A  589  ASP LEU GLU ARG LEU PHE GLN GLU LEU GLN PRO LEU TYR
SEQRES  17 A  589  LEU ASN LEU HIS ALA TYR VAL ARG ARG ALA LEU HIS ARG
SEQRES  18 A  589  HIS TYR GLY ALA GLN HIS ILE ASN LEU GLU GLY PRO ILE
SEQRES  19 A  589  PRO ALA HIS LEU LEU GLY ASN MET TRP ALA GLN THR TRP
SEQRES  20 A  589  SER ASN ILE TYR ASP LEU VAL VAL PRO PHE PRO SER ALA
SEQRES  21 A  589  PRO SER MET ASP THR THR GLU ALA MET LEU LYS GLN GLY
SEQRES  22 A  589  TRP THR PRO ARG ARG MET PHE LYS GLU ALA ASP ASP PHE
SEQRES  23 A  589  PHE THR SER LEU GLY LEU LEU PRO VAL PRO PRO GLU PHE
SEQRES  24 A  589  TRP ASN LYS SER MET LEU GLU LYS PRO THR ASP GLY ARG
SEQRES  25 A  589  GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR ASN
SEQRES  26 A  589  GLY LYS ASP PHE ARG ILE LYS GLN CYS THR THR VAL ASN
SEQRES  27 A  589  LEU GLU ASP LEU VAL VAL ALA HIS HIS GLU MET GLY HIS
SEQRES  28 A  589  ILE GLN TYR PHE MET GLN TYR LYS ASP LEU PRO VAL ALA
SEQRES  29 A  589  LEU ARG GLU GLY ALA ASN PRO GLY PHE HIS GLU ALA ILE
SEQRES  30 A  589  GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO LYS HIS
SEQRES  31 A  589  LEU HIS SER LEU ASN LEU LEU SER SER GLU GLY GLY SER
SEQRES  32 A  589  ASP GLU HIS ASP ILE ASN PHE LEU MET LYS MET ALA LEU
SEQRES  33 A  589  ASP LYS ILE ALA PHE ILE PRO PHE SER TYR LEU VAL ASP
SEQRES  34 A  589  GLN TRP ARG TRP ARG VAL PHE ASP GLY SER ILE THR LYS
SEQRES  35 A  589  GLU ASN TYR ASN GLN GLU TRP TRP SER LEU ARG LEU LYS
SEQRES  36 A  589  TYR GLN GLY LEU CYS PRO PRO VAL PRO ARG THR GLN GLY
SEQRES  37 A  589  ASP PHE ASP PRO GLY ALA LYS PHE HIS ILE PRO SER SER
SEQRES  38 A  589  VAL PRO TYR ILE ARG TYR PHE VAL SER PHE ILE ILE GLN
SEQRES  39 A  589  PHE GLN PHE HIS GLU ALA LEU CYS GLN ALA ALA GLY HIS
SEQRES  40 A  589  THR GLY PRO LEU HIS LYS CYS ASP ILE TYR GLN SER LYS
SEQRES  41 A  589  GLU ALA GLY GLN ARG LEU ALA THR ALA MET LYS LEU GLY
SEQRES  42 A  589  PHE SER ARG PRO TRP PRO GLU ALA MET GLN LEU ILE THR
SEQRES  43 A  589  GLY GLN PRO ASN MET SER ALA SER ALA MET LEU SER TYR
SEQRES  44 A  589  PHE LYS PRO LEU LEU ASP TRP LEU ARG THR GLU ASN GLU
SEQRES  45 A  589  LEU HIS GLY GLU LYS LEU GLY TRP PRO GLN TYR ASN TRP
SEQRES  46 A  589  THR PRO ASN SER
HET    NAG  A 691      14
HET    NAG  A 692      14
HET    NAG  A 693      14
HET    NAG  A 694      14
HET    NAG  A 696      14
HET    NDG  A 695      14
HET    ACT  A 700       4
HET     ZN  A 701       1
HET     CL  A 703       1
HET     CL  A 704       1
HET    NXA  A 702       9
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM     ACT ACETATE ION
HETNAM      ZN ZINC ION
HETNAM      CL CHLORIDE ION
HETNAM     NXA N-CARBOXYALANINE
HETSYN     NAG NAG
FORMUL   2  NAG    5(C8 H15 N O6)
FORMUL   7  NDG    C8 H15 N O6
FORMUL   8  ACT    C2 H3 O2 1-
FORMUL   9   ZN    ZN 2+
FORMUL  10   CL    2(CL 1-)
FORMUL  12  NXA    C4 H7 N O4
FORMUL  13  HOH   *504(H2 O1)
HELIX    1   1 ASP A   40  THR A   71  1                                  32
HELIX    2   2 THR A   74  ARG A  100  1                                  27
HELIX    3   3 LYS A  101  LEU A  107  5                                   7
HELIX    4   4 ASN A  109  GLN A  120  1                                  12
HELIX    5   5 LEU A  122  LEU A  127  5                                   6
HELIX    6   6 PRO A  128  VAL A  148  1                                  21
HELIX    7   7 PRO A  163  SER A  172  1                                  10
HELIX    8   8 LYS A  174  LEU A  210  1                                  37
HELIX    9   9 ASP A  215  SER A  222  1                                   8
HELIX   10  10 MET A  223  GLU A  225  5                                   3
HELIX   11  11 SER A  228  GLY A  260  1                                  33
HELIX   12  12 TRP A  283  ASN A  285  5                                   3
HELIX   13  13 ILE A  286  VAL A  291  1                                   6
HELIX   14  14 ASP A  300  GLN A  308  1                                   9
HELIX   15  15 THR A  311  LEU A  326  1                                  16
HELIX   16  16 PRO A  332  SER A  339  1                                   8
HELIX   17  17 ASN A  374  TYR A  394  1                                  21
HELIX   18  18 PRO A  398  ARG A  402  5                                   5
HELIX   19  19 ASN A  406  LEU A  430  1                                  25
HELIX   20  20 SER A  439  ASP A  473  1                                  35
HELIX   21  21 ASN A  480  GLY A  494  1                                  15
HELIX   22  22 PHE A  506  LYS A  511  5                                   6
HELIX   23  23 TYR A  520  ALA A  541  1                                  22
HELIX   24  24 PRO A  546  CYS A  550  5                                   5
HELIX   25  25 SER A  555  LEU A  568  1                                  14
HELIX   26  26 PRO A  573  GLY A  583  1                                  11
HELIX   27  27 ALA A  589  HIS A  610  1                                  22
SHEET    1  AA 2 ALA A 149  HIS A 153  0
SHEET    2  AA 2 SER A 157  LEU A 161 -1  O  LEU A 159   N  VAL A 151
SHEET    1  AB 2 ILE A 270  ALA A 272  0
SHEET    2  AB 2 LEU A 495  CYS A 496  1  N  CYS A 496   O  ILE A 270
SHEET    1  AC 2 SER A 355  PHE A 359  0
SHEET    2  AC 2 ASP A 364  LYS A 368 -1  O  ARG A 366   N  TRP A 357
SSBOND   1 CYS A  152    CYS A  158                          1555   1555  2.03
SSBOND   2 CYS A  352    CYS A  370                          1555   1555  2.03
SSBOND   3 CYS A  538    CYS A  550                          1555   1555  2.03
LINK         ND2 ASN A  72                 C1  NAG A 691     1555   1555  1.45
LINK         ND2 ASN A  72                 O5  NAG A 691     1555   1555  1.88
LINK         ND2 ASN A  90                 C1  NAG A 692     1555   1555  1.45
LINK         ND2 ASN A 109                 C1  NAG A 693     1555   1555  1.45
LINK         ND2 ASN A 155                 C1  NAG A 694     1555   1555  1.45
LINK         ND2 ASN A 337                 C1  NDG A 695     1555   1555  1.45
LINK         ND2 ASN A 586                 C1  NAG A 696     1555   1555  1.46
LINK        ZN    ZN A 701                 NE2 HIS A 387     1555   1555  2.06
LINK        ZN    ZN A 701                 OE1 GLU A 411     1555   1555  1.97
LINK        ZN    ZN A 701                 O   ACT A 700     1555   1555  2.60
LINK        ZN    ZN A 701                 OXT ACT A 700     1555   1555  2.06
LINK        ZN    ZN A 701                 NE2 HIS A 383     1555   1555  2.02
CISPEP   1 GLU A  162    PRO A  163          0         0.16
SITE     1 AC1  5 ASN A  72  THR A  74  GLU A  76  ASP A 346
SITE     2 AC1  5 ARG A 348
SITE     1 AC2  1 ASN A  90
SITE     1 AC3  2 ASN A 109  ILE A 112
SITE     1 AC4  3 HIS A 153  ASN A 155  SER A 157
SITE     1 AC5  4 THR A 502  ASN A 586  HOH A2221  HOH A2503
SITE     1 AC6  1 ASN A 337
SITE     1 AC7  9 ALA A 354  HIS A 383  GLU A 384  HIS A 387
SITE     2 AC7  9 GLU A 411  TYR A 523   ZN A 701  NXA A 702
SITE     3 AC7  9 HOH A2317
SITE     1 AC8  4 HIS A 383  HIS A 387  GLU A 411  ACT A 700
SITE     1 AC9  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489
SITE     1 BC1  6 TYR A 224  PRO A 407  PRO A 519  ILE A 521
SITE     2 BC1  6 ARG A 522  HOH A2195
SITE     1 BC2 10 GLN A 281  HIS A 353  GLU A 384  LYS A 511
SITE     2 BC2 10 HIS A 513  TYR A 520  TYR A 523  ACT A 700
SITE     3 BC2 10 HOH A2424  HOH A2504
CRYST1   56.620   85.060  133.790  90.00  90.00  90.00 P 21 21 21    4
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      0.017662  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011756  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007474        0.00000
      
PROCHECK
Go to PROCHECK summary
 References