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4QAX

Crystal structure of post-catalytic binary complex of Phosphoglycerate mutase from Staphylococcus aureus

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004619molecular_functionphosphoglycerate mutase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006007biological_processglucose catabolic process
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0030145molecular_functionmanganese ion binding
A0043937biological_processregulation of sporulation
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 601
ChainResidue
AASP397
AHIS401
AHIS456
AHOH701
AHOH702
AHOH703

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 602
ChainResidue
AHIS439
AASP12
ASER62
AASP438

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 2PG A 603
ChainResidue
AHIS123
AARG153
AASP154
AARG185
AARG191
AARG257
AASP259
AARG260

Functional Information from PROSITE/UniProt
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. IEASGLDV
ChainResidueDetails
AILE45-VAL52

245663

PDB entries from 2025-12-03

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