Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6G1J

Phosphotriesterase PTE_C23M_1

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
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue FMT A 401
ChainResidue
AHIS55
AHOH502
AHIS57
ATRP131
ALYS169
AHIS201
AHIS230
AZN402
AZN403
AIMD404

site_idAC2
Number of Residues6
Detailsbinding site for residue ZN A 402
ChainResidue
AHIS55
AHIS57
AASP301
AFMT401
AIMD404
AHOH502

site_idAC3
Number of Residues6
Detailsbinding site for residue ZN A 403
ChainResidue
AHIS201
AHIS230
AFMT401
AIMD404
AHOH501
AHOH502

site_idAC4
Number of Residues7
Detailsbinding site for residue IMD A 404
ChainResidue
AHIS57
AASP301
AFMT401
AZN402
AZN403
AHOH501
AHOH502

site_idAC5
Number of Residues7
Detailsbinding site for residue GOL A 405
ChainResidue
ATYR156
AGLY157
AGLU159
AASP160
ATHR161
AGLY162
AHOH510

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 406
ChainResidue
AALA63
AGLY64
AARG67
AARG108
AGLU159
AHOH536
AHOH609

site_idAC7
Number of Residues4
Detailsbinding site for residue GOL A 407
ChainResidue
AARG139
ATHR177
APRO178
APHE179

site_idAC8
Number of Residues7
Detailsbinding site for residue GOL A 408
ChainResidue
ASER75
AARG76
AALA77
AARG363
AHOH542
AHOH599
AHOH645

site_idAC9
Number of Residues4
Detailsbinding site for residue SO4 A 409
ChainResidue
ATRP277
AGLN278
AARG331
AHOH557

site_idAD1
Number of Residues4
Detailsbinding site for residue SO4 A 410
ChainResidue
ALYS294
ATHR352
AARG356
AHOH555

site_idAD2
Number of Residues1
Detailsbinding site for residue ZN A 411
ChainResidue
ATYR156

site_idAD3
Number of Residues6
Detailsbinding site for residue E8N A 413
ChainResidue
AGLU144
ASER342
ATHR345
AHOH597
AHOH627
AHOH650

site_idAD4
Number of Residues3
Detailsbinding site for residue SO4 A 414
ChainResidue
ALYS82
AARG85
AARG89

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 Residues5
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
AHIS57
AHIS201
AHIS230
AASP301

site_idSWS_FT_FI2
Number of Residues1
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

site_idSWS_FT_FI3
Number of Residues1
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

Catalytic Information from CSA
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
AGLY254hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
AASP301hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon