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4HI1

Crystal structure of acylphosphatase C20R mutant from Vibrio cholerae0395

Functional Information from GO Data
ChainGOidnamespacecontents
A0003998molecular_functionacylphosphatase activity
A0016787molecular_functionhydrolase activity
B0003998molecular_functionacylphosphatase activity
B0016787molecular_functionhydrolase activity
C0003998molecular_functionacylphosphatase activity
C0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MOO A 101
ChainResidue
AGLY16
BHOH209
AVAL17
AGLY18
APHE19
AARG20
ATYR21
AHOH201
AHOH216
AHOH220

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 102
ChainResidue
AHOH224
CLYS37
CLEU39
CASN40

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MOO B 101
ChainResidue
BGLY18
BPHE19
BARG20
BTYR21
BHOH202
BHOH204
BHOH206
BHOH227
CGLY31

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 102
ChainResidue
AHIS25
ALYS29
BHIS25
BLYS29
BHOH241
CHIS25
CLYS29

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 103
ChainResidue
ALEU39
AASN40
BHOH224
BHOH284

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MOO C 101
ChainResidue
AGLY31
AHOH256
CGLY16
CVAL17
CGLY18
CPHE19
CARG20
CTYR21
CILE90
CHOH201
CHOH205
CHOH215

Functional Information from PROSITE/UniProt
site_idPS00150
Number of Residues11
DetailsACYLPHOSPHATASE_1 Acylphosphatase signature 1. VsGhVQGVgFR
ChainResidueDetails
AVAL10-ARG20

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00520
ChainResidueDetails
AASN38
BASN38
CASN38

222926

PDB entries from 2024-07-24

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