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1BF6

PHOSPHOTRIESTERASE HOMOLOGY PROTEIN FROM ESCHERICHIA COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0009056biological_processcatabolic process
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0046872molecular_functionmetal ion binding
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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
AHIS12
AHIS14
AGLU125
AASP243
AZN293

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 293
ChainResidue
AZN1
AGLU125
AHIS158
AHIS186

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 293
ChainResidue
BHIS12
BHIS14
BGLU125
BASP243
BZN294

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 294
ChainResidue
BGLU125
BHIS158
BHIS186
BZN293

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 294
ChainResidue
ASER162
ATHR163
AMET164
ALYS190
AASN195
AHOH759

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 295
ChainResidue
ALYS213
ATYR216
ATHR245
AARG246
AHIS249

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 720
ChainResidue
BASP201
BLEU202
BHOH324

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 529
ChainResidue
AARG57
ATYR58
AARG96
AHOH749

Functional Information from PROSITE/UniProt
site_idPS01322
Number of Residues9
DetailsPHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GyTLaHEHL
ChainResidueDetails
AGLY7-LEU15

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:30277746, ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6, ECO:0007744|PDB:4LEF
ChainResidueDetails
AHIS12
BHIS158
BHIS186
BASP243
AHIS14
AGLU125
AHIS158
AHIS186
AASP243
BHIS12
BHIS14
BGLU125

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:30277746, ECO:0007744|PDB:4LEF
ChainResidueDetails
AHIS148
BARG181
BASP280
BARG284
AGLY176
AASP178
AARG181
AASP280
AARG284
BHIS148
BGLY176
BASP178

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PDB entries from 2024-07-24

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