Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4OJ3

The crystal structure of V84P 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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 201
ChainResidue
AGLY28
APHE29
AARG30
ALYS31
AHOH301
AHOH307

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 202
ChainResidue
AARG71
AHOH316
AARG30
AARG39
AASN48

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 203
ChainResidue
AGLY22
ALEU23
AVAL24
AGLN25
AILE35
AILE38
AGLY52
BGLU80
BGLU82

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 201
ChainResidue
BGLY28
BPHE29
BARG30
BLYS31
BHOH307
BHOH311
BHOH312
BHOH315
BHOH324

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 202
ChainResidue
BARG30
BARG39
BASN48
BARG71
BHOH326

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 203
ChainResidue
AGLU80
AGLU82
BGLY22
BLEU23
BVAL24
BGLN25
BILE35
BILE38
BGLY52

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

238268

PDB entries from 2025-07-02

PDB statisticsPDBj update infoContact PDBjnumon