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4PZA

The complex structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase Rv2419c with inorganic phosphate

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 PO4 A 601
ChainResidue
AARG10
AHIS11
AARG60
AGLU84
AHIS159
AGLY160
AHOH714
AHOH721
AHOH727

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 B 601
ChainResidue
BARG10
BHIS11
BARG60
BGLU84
BHIS159
BGLY160
BHOH704
BHOH712
BHOH745
BHOH820

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
DetailsActive site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"UniProtKB","id":"P9WIC7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P9WIC7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P9WIC7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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