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4OJG

The crystal structure of V84D mutant of S. solfataricus acylphosphatase

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 Residues11
DetailsBINDING SITE FOR RESIDUE PO4 A 201
ChainResidue
AVAL24
AHOH306
AHOH425
AGLN25
AGLY26
AVAL27
AGLY28
APHE29
AARG30
AASN48
AHOH303

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 201
ChainResidue
ASER66
ALEU69
APHE88
AHOH307
BSER66
BLEU69
BPHE88
BHOH304
BHOH325
BHOH362

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 B 202
ChainResidue
BVAL24
BGLN25
BGLY26
BVAL27
BGLY28
BPHE29
BARG30
BASN48
BHOH322
BHOH384

Functional Information from PROSITE/UniProt
site_idPS00150
Number of Residues11
DetailsACYLPHOSPHATASE_1 Acylphosphatase signature 1. VyGlVQGVgFR
ChainResidueDetails
AVAL20-ARG30

site_idPS00151
Number of Residues17
DetailsACYLPHOSPHATASE_2 Acylphosphatase signature 2. GYAKNlpdGsVevvaeG
ChainResidueDetails
AGLY44-GLY60

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:16287076
ChainResidueDetails
AARG30
AASN48
BARG30
BASN48

222624

PDB entries from 2024-07-17

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