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1I0B

HIGH RESOLUTION STRUCTURE OF THE MANGANESE-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 MN A 401
ChainResidue
AHIS55
AHIS57
AASP301
AFMT369
AMN402
AEDO408
AHOH1010

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 402
ChainResidue
AFMT369
AMN401
AHOH853
AHOH1010
AHOH1012
AHIS201
AHIS230

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN B 401
ChainResidue
BHIS55
BHIS57
BASP301
BFMT369
BMN402
BEDO407
BHOH1009

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN B 402
ChainResidue
BHIS201
BHIS230
BFMT369
BMN401
BHOH1009
BHOH1011
BHOH1015

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 405
ChainResidue
AASN38
AILE154
AGLN155
AARG164
AHOH787
AHOH1014

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA B 406
ChainResidue
BASN38
BILE154
BGLN155
BARG164
BHOH785
BHOH806
BHOH1018

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 407
ChainResidue
BHIS57
BILE106
BTRP131
BFMT369
BMN401
BHOH530
BHOH1011
BHOH1127

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 408
ChainResidue
AHIS57
ATRP131
APHE306
AFMT369
AMN401
AHOH854
AHOH995
AHOH1010
AHOH1012

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 409
ChainResidue
AARG91
BTHR147
BHOH710
BHOH786

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 410
ChainResidue
ALEU182
AHOH558

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 411
ChainResidue
AVAL84
AGLU115
AHOH796

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 412
ChainResidue
AEDO413
AHOH559
AHOH783
AHOH1016
BARG91

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 413
ChainResidue
AEDO412
AHOH1016
BARG91
BASP121
BHOH676

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 414
ChainResidue
BLYS77
BGLU115
BHOH1059

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 415
ChainResidue
BPRO256
BTRP277
BVAL320
BPHE327

site_idBC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO B 416
ChainResidue
AASP133
APRO134
APRO135
BASP133
BPRO134
BPRO135
BHOH472
BHOH475
BHOH836

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 417
ChainResidue
ASER47
AGLU48
AGLY50
AARG96

site_idBC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 418
ChainResidue
BGLY50
BARG96
BHIS123
BHOH636
BHOH989
BSER47
BGLU48

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 419
ChainResidue
AARG41
AGLY42
APRO43
BEDO423

site_idCC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 420
ChainResidue
APHE72
APHE73
AGLY305
APHE306
AMET314
AHOH489

site_idCC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 421
ChainResidue
BPRO70
BGLU71
BSER75
BARG76
BHOH550
BHOH655
BHOH939

site_idCC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 422
ChainResidue
BASN265
BSER267
BVAL310
BTHR311
BASN312
BILE313
BVAL316
BHOH930

site_idCC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 423
ChainResidue
AGLY42
APRO43
AEDO419
AHOH440
AHOH883
AHOH923
BPRO334
BGLU338

site_idCC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 424
ChainResidue
AARG337
AGLN343
AHOH457
BTYR156
BHOH698

site_idCC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 425
ChainResidue
BTHR352
BALA355
BHOH635

site_idCC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 426
ChainResidue
APHE104
AARG108
AGLU159
AHOH476
BGLY64
BARG67
BALA68

site_idCC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 427
ChainResidue
AGLN295
AARG356
AHOH984

site_idDC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 428
ChainResidue
BLYS285
BLYS339
BGLY340
BHOH758

site_idDC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 429
ChainResidue
BGLY74
BALA78
BHOH810

site_idDC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 430
ChainResidue
AGLY74
AALA78
AHOH934

site_idDC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 431
ChainResidue
BARG118
BHOH906

site_idDC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 432
ChainResidue
AGLU210
AALA242
AARG246
AHOH576

site_idDC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEL B 433
ChainResidue
BLYS77
BMET293
BGLY348
BASN353
BARG356

site_idDC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEL A 434
ChainResidue
ALYS77
AMET293
ALYS294
ATHR345
AGLY348
AILE349
AASN353

site_idDC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE FMT A 369
ChainResidue
AHIS55
AHIS57
AILE106
ATRP131
ALYS169
AHIS201
AHIS230
AMN401
AMN402
AEDO408
AHOH1010
AHOH1012

site_idDC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT B 369
ChainResidue
BHIS55
BHIS57
BLYS169
BHIS201
BHIS230
BMN401
BMN402
BEDO407
BHOH1009

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 2024-07-10

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