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1HZY

HIGH RESOLUTION STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE FROM PSEUDOMONAS DIMINUTA

Functional Information from GO Data
ChainGOidnamespacecontents
A0004063molecular_functionaryldialkylphosphatase activity
A0005886cellular_componentplasma membrane
A0008270molecular_functionzinc ion binding
A0009056biological_processcatabolic process
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0046872molecular_functionmetal ion binding
B0004063molecular_functionaryldialkylphosphatase activity
B0005886cellular_componentplasma membrane
B0008270molecular_functionzinc ion binding
B0009056biological_processcatabolic process
B0016787molecular_functionhydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AHIS55
AHIS57
AASP301
AFMT369
AZN402
AEDO408
AHOH876

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
AFMT369
AZN401
AHOH876
AHOH897
AHIS201
AHIS230

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN B 401
ChainResidue
BHIS55
BHIS57
BASP301
BFMT369
BZN402
BEDO407
BHOH831

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 402
ChainResidue
BHIS201
BHIS230
BFMT369
BZN401
BHOH831
BHOH919

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 405
ChainResidue
AASN38
AILE154
AHOH436
AHOH815
AHOH963

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 406
ChainResidue
BASN38
BILE154
BHOH635
BHOH812
BHOH873

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 407
ChainResidue
BHIS57
BILE106
BTRP131
BFMT369
BZN401
BEDO422
BEDO423
BHOH919

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 408
ChainResidue
AHIS57
AILE106
ATRP131
APHE306
AFMT369
AZN401
AEDO425
AEDO426
AHOH897

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 409
ChainResidue
AARG91
BTHR147
BHOH722
BHOH813
BHOH1060

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 410
ChainResidue
ALEU182
AHOH541
AHOH838
AHOH853
AHOH1177

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 411
ChainResidue
AGLU115
AHOH498
AHOH890

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 412
ChainResidue
ATHR147
AARG189
AHOH563
AHOH808
AHOH906
BARG91

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 413
ChainResidue
BARG76
BGLU115

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 414
ChainResidue
BGLY305
BPHE306
BMET314
BHOH779

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 415
ChainResidue
BPRO256
BTRP277
BVAL320
BPHE327
BHOH825
BHOH1178

site_idBC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 416
ChainResidue
AASP133
APRO134
APRO135
AHOH469
AHOH472
AHOH537
BASP133
BPRO134
BPRO135

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 417
ChainResidue
AVAL351
AHOH450
AHOH993
AHOH1119

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 418
ChainResidue
AALA270
AALA266
ASER269

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 419
ChainResidue
ASER276
ATHR279
AHOH594

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 420
ChainResidue
APRO256
ATRP277
AVAL320
APHE327
AHOH877

site_idCC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 421
ChainResidue
BTRP131
BPHE132
BPRO134
BTHR177
BGLN180
BHOH700
BHOH702

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 422
ChainResidue
BSER308
BTYR309
BEDO407
BHOH920
BHOH1191

site_idCC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 423
ChainResidue
BHIS257
BASP301
BEDO407
BHOH831
BHOH1124

site_idCC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 424
ChainResidue
AHOH1120
BSER47
BGLU48
BGLY50
BARG96

site_idCC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 425
ChainResidue
AHIS254
AHIS257
AASP301
AEDO408

site_idCC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 426
ChainResidue
ASER308
ATYR309
AEDO408
AHOH1190

site_idCC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEL B 427
ChainResidue
BLYS77
BMET293
BTHR345
BGLY348
BASN353

site_idDC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEL A 428
ChainResidue
ALYS77
AMET293
ALYS294
ATHR345
AGLY348
AILE349
AASN353

site_idDC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FMT A 369
ChainResidue
AHIS55
AHIS57
AILE106
ALYS169
AHIS201
AHIS230
AZN401
AZN402
AEDO408
AHOH876

site_idDC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT B 369
ChainResidue
BHIS55
BHIS57
BLYS169
BHIS201
BHIS230
BZN401
BZN402
BEDO407
BHOH831

Functional Information from PROSITE/UniProt
site_idPS01322
Number of Residues9
DetailsPHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GfTLtHEHI
ChainResidueDetails
AGLY50-ILE58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL
ChainResidueDetails
AHIS55
BASP301
AHIS57
AHIS201
AHIS230
AASP301
BHIS55
BHIS57
BHIS201
BHIS230

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: via carbamate group => ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL
ChainResidueDetails
ALYS169
BLYS169

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000255|PROSITE-ProRule:PRU00679, ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL
ChainResidueDetails
ALYS169
BLYS169

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ez2
ChainResidueDetails
AHIS254
AASP233
AASP301

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ez2
ChainResidueDetails
BHIS254
BASP233
BASP301

site_idMCSA1
Number of Residues8
DetailsM-CSA 159
ChainResidueDetails
AHIS55metal ligand
AHIS57metal ligand
ALYS169metal ligand
AHIS201metal ligand
AHIS230metal ligand
AASP233hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS254hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
AASP301hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

site_idMCSA2
Number of Residues8
DetailsM-CSA 159
ChainResidueDetails
BHIS55metal ligand
BHIS57metal ligand
BLYS169metal ligand
BHIS201metal ligand
BHIS230metal ligand
BASP233hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BHIS254hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
BASP301hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

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PDB entries from 2024-07-24

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