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1W2I

Crystal structuore of acylphosphatase from Pyrococcus horikoshii complexed with formate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003998molecular_functionacylphosphatase activity
A0016787molecular_functionhydrolase activity
B0003998molecular_functionacylphosphatase activity
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A1092
ChainResidue
AGLY18
APHE19
AARG20
ATRP21
AHOH2022
AHOH2026

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A1093
ChainResidue
BGLY18
BTRP21
BSER22
AARG20
AGLN80
AHOH2107

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT B1092
ChainResidue
BGLY18
BPHE19
BARG20
BTRP21
BHOH2021
BHOH2025

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT B1093
ChainResidue
BARG88

Functional Information from PROSITE/UniProt
site_idPS00150
Number of Residues11
DetailsACYLPHOSPHATASE_1 Acylphosphatase signature 1. IyGrVQGVgFR
ChainResidueDetails
AILE10-ARG20

site_idPS00151
Number of Residues17
DetailsACYLPHOSPHATASE_2 Acylphosphatase signature 2. GWVRNlpdGsVeavleG
ChainResidueDetails
AGLY34-GLY50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:15779887
ChainResidueDetails
AARG20
AASN38
BARG20
BASN38

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2acy
ChainResidueDetails
AASN38
AARG20

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2acy
ChainResidueDetails
BASN38
BARG20

222415

PDB entries from 2024-07-10

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