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1V3Z

Crystal Structure of Acylphosphatase from Pyrococcus horikoshii

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 Residues7
DetailsBINDING SITE FOR RESIDUE K B 501
ChainResidue
BGLN64
BPRO66
BPRO67
BALA69
BHOH549
BHOH553
BHOH563

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 502
ChainResidue
APRO67
AALA69
AHOH551
AGLN64
APRO66

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 503
ChainResidue
AGLY18
APHE19
AARG20

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 504
ChainResidue
BGLY18
BPHE19
BARG20
BTRP21

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

224931

PDB entries from 2024-09-11

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