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4QIH

The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase Rv2419c complexes with VO3

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0050531molecular_functionmannosyl-3-phosphoglycerate phosphatase activity
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0050531molecular_functionmannosyl-3-phosphoglycerate phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE VN3 A 601
ChainResidue
AARG10
AHIS11
AASN17
AGLN23
AARG60
AGLU84
AHIS159
AGLY160
AHOH766

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE VN3 B 601
ChainResidue
BARG10
BHIS11
BASN17
BGLN23
BARG60
BGLU84
BHIS159
BGLY160
BHOH720

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. MlRHGQtDyN
ChainResidueDetails
AMET8-ASN17

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000250|UniProtKB:P9WIC7
ChainResidueDetails
AHIS11
BHIS11

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P9WIC7
ChainResidueDetails
AGLU84
BGLU84

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WIC7
ChainResidueDetails
AARG10
AARG60
AHIS159
BARG10
BARG60
BHIS159

218853

數據於2024-04-24公開中

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