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1PSC

PHOSPHOTRIESTERASE FROM PSEUDOMONAS DIMINUTA

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0009056biological_processcatabolic process
A0016788molecular_functionhydrolase activity, acting on ester bonds
B0008270molecular_functionzinc ion binding
B0009056biological_processcatabolic process
B0016788molecular_functionhydrolase activity, acting on ester bonds
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 801
ChainResidue
AHIS55
AHIS57
AASP301
AFMT901
AHOH912

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 802
ChainResidue
AHOH912
AHOH985
AHIS201
AHIS230
AFMT901
AHOH905

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD B 803
ChainResidue
BHIS55
BHIS57
BASP301
BFMT902
BHOH1004

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD B 804
ChainResidue
BHIS201
BHIS230
BFMT902
BHOH1002
BHOH1003
BHOH1004

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EBP A 900
ChainResidue
APHE51
AGLU71
BLEU151
BARG152
BGLN155
BTYR156

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EBP B 901
ChainResidue
ALEU151
AARG152
AGLN155
ATYR156
BPHE51
BHOH1038
BHOH1105

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 901
ChainResidue
AHIS55
AHIS57
ALYS169
AHIS201
AHIS230
ACD801
ACD802

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT B 902
ChainResidue
BHIS55
BHIS57
BLYS169
BHIS201
BHIS230
BCD803
BCD804

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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