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3URA

Crystal Structure of PTE mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T

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 Residues9
DetailsBINDING SITE FOR RESIDUE IMD A 1372
ChainResidue
AHIS230
AASP232
AASP233
AASP253
AGLY254
ATRP257
AARG280
AASP301
AHOH1135

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 801
ChainResidue
AKCX169
AHIS201
AHIS230
AHOH1238
AHOH1256
AHOH1310

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 802
ChainResidue
AHIS55
AHIS57
AKCX169
AASP301
AHOH1310

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO B 803
ChainResidue
BHIS55
BHIS57
BKCX169
BASP301
BCO804
BHOH1324

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO B 804
ChainResidue
BKCX169
BHIS201
BHIS230
BCO803
BHOH1325

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
AKCX169
BKCX169

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
AKCX169
BKCX169

Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 159
ChainResidueDetails
AHIS55metal ligand
AHIS57metal ligand
AKCX169metal ligand
AHIS201metal ligand
AHIS230metal ligand
AASP233hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLY254hydrogen 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
BKCX169metal ligand
BHIS201metal ligand
BHIS230metal ligand
BASP233hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLY254hydrogen 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 2024-11-20

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