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

5KGM

2.95A resolution structure of Apo independent phosphoglycerate mutase from C. elegans (monoclinic form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004619molecular_functionphosphoglycerate mutase activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0006007biological_processglucose catabolic process
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0030145molecular_functionmanganese ion binding
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004619molecular_functionphosphoglycerate mutase activity
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0006007biological_processglucose catabolic process
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0030145molecular_functionmanganese ion binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 601
ChainResidue
AARG97
AASN336

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 602
ChainResidue
AARG216
AARG284

site_idAC3
Number of Residues3
Detailsbinding site for residue MN A 603
ChainResidue
AASP426
AHIS430
AHIS485

site_idAC4
Number of Residues5
Detailsbinding site for residue ZN A 604
ChainResidue
ALYS359
AASP467
AHIS468
AASP37
ASER86

site_idAC5
Number of Residues2
Detailsbinding site for residue CL B 601
ChainResidue
BARG97
BASN336

site_idAC6
Number of Residues2
Detailsbinding site for residue CL B 602
ChainResidue
BARG216
BARG284

site_idAC7
Number of Residues3
Detailsbinding site for residue MN B 603
ChainResidue
BASP426
BHIS430
BHIS485

site_idAC8
Number of Residues5
Detailsbinding site for residue ZN B 604
ChainResidue
BASP37
BSER86
BLYS359
BASP467
BHIS468

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"Q9X519","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9X519","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

PDB statisticsPDBj update infoContact PDBjnumon