spacer
spacer

PDBsum entry 1o86

Go to PDB code: 
Top Page protein ligands metals links
Hydrolase/hydrolase inhibitor PDB id
1o86
Jmol
Contents
Protein chain
575 a.a. *
Ligands
GLY
LPR
Metals
_CL ×2
_ZN
Waters ×570
* Residue conservation analysis
HEADER    HYDROLASE/HYDROLASE INHIBITOR           25-NOV-02   1O86
TITLE     CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERTING ENZYME IN COMPLEX
TITLE    2 WITH LISINOPRIL.
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, PEPTIDYL DIPEPTIDASE, TYPE-I MEMBRANE-ANCHORED
KEYWDS   2 PROTEIN, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.NATESH,S.L.U.SCHWAGER,E.D.STURROCK,K.R.ACHARYA
REVDAT   4   13-JUL-11 1O86    1       VERSN
REVDAT   3   24-FEB-09 1O86    1       VERSN
REVDAT   2   06-MAR-06 1O86    1       TITLE  REMARK
REVDAT   1   07-FEB-03 1O86    0
JRNL        AUTH   R.NATESH,S.L.U.SCHWAGER,E.D.STURROCK,K.R.ACHARYA
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN ANGIOTENSIN-CONVERTING
JRNL        TITL 2 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.    2.00 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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.14
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.3
REMARK   3   NUMBER OF REFLECTIONS             : 79258
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) : 0.180
REMARK   3   FREE R VALUE                     : 0.220
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.700
REMARK   3   FREE R VALUE TEST SET COUNT      : 3094
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          : 36
REMARK   3   SOLVENT ATOMS            : 570
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 19.50
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.60
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) : 0.20
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.33
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.21
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.24
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.53
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.84
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 1O86 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-NOV-02.
REMARK 100 THE PDBE ID CODE IS EBI-11733.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-01
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               : ESRF
REMARK 200  BEAMLINE                       : BM14
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537,1.2825,1.2832
REMARK 200  MONOCHROMATOR                  : SI
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79319
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     (%) : 95.9
REMARK 200  DATA REDUNDANCY                : 2.000
REMARK 200  R MERGE                    (I) : 0.05800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.30
REMARK 200  R MERGE FOR SHELL          (I) : 0.23800
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: CCP4, CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000/SODIUM ACETATE., PH 4.70
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       28.23500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.99500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.45000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.99500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.23500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.45000
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 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 OF 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
REMARK 470     GLN A 618    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
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       77.76   -172.13
REMARK 500    GLU A 123     -135.46     55.90
REMARK 500    ASN A 155      -85.04    -69.73
REMARK 500    ASP A 164      -70.08    -49.88
REMARK 500    LYS A 363      -39.41   -131.28
REMARK 500    ASN A 431       35.29     70.27
REMARK 500    ASP A 453      -64.92    -94.98
REMARK 500    GLN A 554       19.92     55.84
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 A2022        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH A2027        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH A2054        DISTANCE =  5.60 ANGSTROMS
REMARK 525    HOH A2265        DISTANCE =  6.19 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     GLY A 2000
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 387   NE2
REMARK 620 2 LPR A 702   O2   90.0
REMARK 620 3 LPR A 702   O3  122.9  53.0
REMARK 620 4 GLU A 411   OE1 110.4 151.8  98.8
REMARK 620 5 HIS A 383   NE2 109.6  98.7 116.9  92.7
REMARK 620 N                    1     2     3     4
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: [N2-[(S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-PROLINE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630   M RES C SSSEQI
REMARK 630     LPR A   702
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP:    CLT LYS PRO
REMARK 630 DETAILS: NULL
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 ZN A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LPR A 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1O8A   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERTING ENZYME
REMARK 900 (NATIVE).
DBREF  1O86 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    GLY  A2000       4
HET     ZN  A 701       1
HET    LPR  A 702      29
HET     CL  A 703       1
HET     CL  A 704       1
HETNAM     GLY GLYCINE
HETNAM      ZN ZINC ION
HETNAM     LPR [N2-[(S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-PROLINE
HETNAM      CL CHLORIDE ION
HETSYN     LPR LISINOPRIL
FORMUL   2  GLY    C2 H5 N O2
FORMUL   3   ZN    ZN 2+
FORMUL   4  LPR    C21 H31 N3 O5
FORMUL   5   CL    2(CL 1-)
FORMUL   7  HOH   *570(H2 O)
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  ALA A  149  1                                  22
HELIX    7   7 PRO A  163  SER A  172  1                                  10
HELIX    8   8 LYS A  174  ASN A  211  1                                  38
HELIX    9   9 ASP A  215  SER A  222  1                                   8
HELIX   10  12 MET A  223  GLU A  225  5                                   3
HELIX   11  13 SER A  228  GLY A  260  1                                  33
HELIX   12  15 TRP A  283  ASN A  285  5                                   3
HELIX   13  16 ILE A  286  VAL A  291  1                                   6
HELIX   14  17 ASP A  300  GLN A  308  1                                   9
HELIX   15  18 THR A  311  LEU A  326  1                                  16
HELIX   16  19 PRO A  332  SER A  339  1                                   8
HELIX   17  20 ASN A  374  TYR A  394  1                                  21
HELIX   18  21 PRO A  398  ARG A  402  5                                   5
HELIX   19  22 ASN A  406  LEU A  430  1                                  25
HELIX   20  24 SER A  439  ASP A  473  1                                  35
HELIX   21  25 ASN A  480  GLY A  494  1                                  15
HELIX   22  26 PHE A  506  LYS A  511  5                                   6
HELIX   23  27 TYR A  520  ALA A  541  1                                  22
HELIX   24  28 PRO A  546  CYS A  550  5                                   5
HELIX   25  29 SER A  555  LEU A  568  1                                  14
HELIX   26  30 PRO A  573  GLY A  583  1                                  11
HELIX   27  31 ALA A  589  HIS A  610  1                                  22
SHEET    1  AA 2 THR A 150  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        ZN    ZN A 701                 NE2 HIS A 387     1555   1555  2.07
LINK        ZN    ZN A 701                 O2  LPR A 702     1555   1555  2.61
LINK        ZN    ZN A 701                 O3  LPR A 702     1555   1555  2.14
LINK        ZN    ZN A 701                 OE1 GLU A 411     1555   1555  2.00
LINK        ZN    ZN A 701                 NE2 HIS A 383     1555   1555  2.04
CISPEP   1 GLU A  162    PRO A  163          0         0.61
SITE     1 AC1  4 HIS A 383  HIS A 387  GLU A 411  LPR A 702
SITE     1 AC2  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489
SITE     1 AC3  5 TYR A 224  PRO A 407  PRO A 519  ILE A 521
SITE     2 AC3  5 ARG A 522
SITE     1 AC4  4 ASP A 415  ASP A 453  LYS A 454  PHE A 527
SITE     1 AC5 17 GLU A 162  GLN A 281  HIS A 353  ALA A 354
SITE     2 AC5 17 HIS A 383  GLU A 384  HIS A 387  GLU A 411
SITE     3 AC5 17 LYS A 511  HIS A 513  TYR A 520  TYR A 523
SITE     4 AC5 17  ZN A 701  HOH A2392  HOH A2568  HOH A2569
SITE     5 AC5 17 HOH A2570
CRYST1   56.470   84.900  133.990  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      0.017708  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011778  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007463        0.00000
      
PROCHECK
Go to PROCHECK summary
 References