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PDBsum entry 1uze

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Metalloprotease PDB id
1uze
Jmol
Contents
Protein chain
575 a.a. *
Ligands
GLY
EAL
Metals
_ZN
_CL ×2
Waters ×456
* Residue conservation analysis
HEADER    METALLOPROTEASE                         11-MAR-04   1UZE
TITLE     COMPLEX OF THE ANTI-HYPERTENSIVE DRUG ENALAPRILAT AND THE
TITLE    2 HUMAN TESTICULAR ANGIOTENSIN I-CONVERTING ENZYME
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ANGIOTENSIN CONVERTING ENZYME;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 68-656;
COMPND   5 SYNONYM: ACE-T, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II;
COMPND   6 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: CHINESE HAMSTER OVARY;
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: CHO;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PLEN
KEYWDS    METALLOPROTEASE, ANGIOTENSIN CONVERTING ENZYME, INHIBITOR,
KEYWDS   2 ENALAPRILAT, ZINC DEPENDANT PEPTIDASE, ANTI-HYPERTENSIVE
KEYWDS   3 DRUG
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.NATESH,S.L.U.SCHWAGER,H.R.EVANS,E.D.STURROCK,K.R.ACHARYA
REVDAT   3   24-FEB-09 1UZE    1       VERSN
REVDAT   2   06-MAR-06 1UZE    1       REMARK
REVDAT   1   16-JUL-04 1UZE    0
JRNL        AUTH   R.NATESH,S.L.U.SCHWAGER,H.R.EVANS,E.D.STURROCK,
JRNL        AUTH 2 K.R.ACHARYA
JRNL        TITL   STRUCTURAL DETAILS ON THE BINDING OF
JRNL        TITL 2 ANTIHYPERTENSIVE DRUGS CAPTOPRIL AND ENALAPRILAT
JRNL        TITL 3 TO HUMAN TESTICULAR ANGIOTENSIN I-CONVERTING
JRNL        TITL 4 ENZYME
JRNL        REF    BIOCHEMISTRY                  V.  43  8718 2004
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   15236580
JRNL        DOI    10.1021/BI049480N
REMARK   2
REMARK   2 RESOLUTION.    1.82 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
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) : 1.82
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99
REMARK   3   NUMBER OF REFLECTIONS             : 58651
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.188
REMARK   3   FREE R VALUE                     : 0.211
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.5
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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            : 4662
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 32
REMARK   3   SOLVENT ATOMS            : 456
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
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) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.2
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
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  : NULL
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1UZE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAR-04.
REMARK 100 THE PDBE ID CODE IS EBI-14774.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 4.60
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                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58651
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : 8.000
REMARK 200  R MERGE                    (I) : 0.08900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 21.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.89
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.40600
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       28.36000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.86500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.67500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.86500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.36000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.67500
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 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     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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    LEU A 463   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES
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 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       73.38   -172.34
REMARK 500    GLU A 123     -135.39     55.36
REMARK 500    LYS A 363      -35.93   -134.44
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 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 EAL A3002   O2
REMARK 620 2 EAL A3002   O3   53.0
REMARK 620 3 HIS A 387   NE2  92.6 125.2
REMARK 620 4 GLU A 411   OE1 156.3 103.5 105.7
REMARK 620 5 HIS A 383   NE2  98.6 116.4 109.2  89.6
REMARK 620 N                    1     2     3     4
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 EAL A3002
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.
REMARK 900 RELATED ID: 1O8A   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN
REMARK 900  CONVERTING ENZYME (NATIVE).
REMARK 900 RELATED ID: 1UZF   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN
REMARK 900  CONVERTING ENZYME IN COMPLEX WITH CAPTOPRIL
DBREF  1UZE 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     ZN  A 701       1
HET     CL  A 703       1
HET     CL  A 704       1
HET    GLY  A2000       4
HET    EAL  A3002      25
HETNAM      ZN ZINC ION
HETNAM      CL CHLORIDE ION
HETNAM     GLY GLYCINE
HETNAM     EAL 1-((2S)-2-{[(1S)-1-CARBOXY-3-PHENYLPROPYL]
HETNAM   2 EAL  AMINO}PROPANOYL)-L-PROLINE
HETSYN     EAL ENALAPRILAT INHIBITOR
FORMUL   2   ZN    ZN 2+
FORMUL   3   CL    2(CL 1-)
FORMUL   5  GLY    C2 H5 N O2
FORMUL   6  EAL    C18 H24 N2 O5
FORMUL   7  HOH   *456(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 ASP A  103  LEU A  107  5                                   5
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  ALA A  189  1                                  16
HELIX    9   9 ALA A  189  LEU A  194  1                                   6
HELIX   10  10 PHE A  196  ASN A  211  1                                  16
HELIX   11  11 ASP A  215  SER A  222  1                                   8
HELIX   12  12 MET A  223  GLU A  225  5                                   3
HELIX   13  13 SER A  228  LEU A  240  1                                  13
HELIX   14  14 LEU A  240  GLY A  260  1                                  21
HELIX   15  15 TRP A  283  ASN A  285  5                                   3
HELIX   16  16 ILE A  286  VAL A  291  1                                   6
HELIX   17  17 ASP A  300  GLN A  308  1                                   9
HELIX   18  18 THR A  311  LEU A  326  1                                  16
HELIX   19  19 PRO A  332  SER A  339  1                                   8
HELIX   20  20 ASN A  374  TYR A  394  1                                  21
HELIX   21  21 PRO A  398  ARG A  402  5                                   5
HELIX   22  22 ASN A  406  SER A  422  1                                  17
HELIX   23  23 THR A  423  LEU A  430  1                                   8
HELIX   24  24 SER A  439  ASP A  473  1                                  35
HELIX   25  25 ASN A  480  GLY A  494  1                                  15
HELIX   26  26 PHE A  506  LYS A  511  5                                   6
HELIX   27  27 TYR A  520  ALA A  541  1                                  22
HELIX   28  28 PRO A  546  CYS A  550  5                                   5
HELIX   29  29 SER A  555  LYS A  567  1                                  13
HELIX   30  30 PRO A  573  GLY A  583  1                                  11
HELIX   31  31 ALA A  589  HIS A  610  1                                  22
SHEET    1  AA 2 THR A 150  CYS A 152  0
SHEET    2  AA 2 CYS A 158  GLN A 160 -1  O  LEU A 159   N  VAL A 151
SHEET    1  AB 2 ILE A 270  PRO A 271  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  ASP A 358  0
SHEET    2  AC 2 PHE A 365  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                 O2  EAL A3002     1555   1555  2.66
LINK        ZN    ZN A 701                 O3  EAL A3002     1555   1555  2.02
LINK        ZN    ZN A 701                 NE2 HIS A 387     1555   1555  2.05
LINK        ZN    ZN A 701                 OE1 GLU A 411     1555   1555  1.89
LINK        ZN    ZN A 701                 NE2 HIS A 383     1555   1555  2.10
CISPEP   1 GLU A  162    PRO A  163          0         0.19
SITE     1 AC1  4 HIS A 383  HIS A 387  GLU A 411  EAL A3002
SITE     1 AC2  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489
SITE     1 AC3  6 TYR A 224  PRO A 407  PRO A 519  ILE A 521
SITE     2 AC3  6 ARG A 522  HOH A2172
SITE     1 AC4  7 VAL A 379  ASP A 415  ASP A 453  LYS A 454
SITE     2 AC4  7 PHE A 527  HOH A2334  EAL A3002
SITE     1 AC5 18 GLN A 281  HIS A 353  ALA A 354  HIS A 383
SITE     2 AC5 18 GLU A 384  HIS A 387  GLU A 411  LYS A 511
SITE     3 AC5 18 PHE A 512  HIS A 513  VAL A 518  TYR A 520
SITE     4 AC5 18 TYR A 523   ZN A 701  GLY A2000  HOH A2281
SITE     5 AC5 18 HOH A2455  HOH A2456
CRYST1   56.720   85.350  133.730  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      0.017630  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011716  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007478        0.00000
      
PROCHECK
Go to PROCHECK summary
 References