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

2G4J

Anomalous substructure of Glucose isomerase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0009045molecular_functionxylose isomerase activity
A0016853molecular_functionisomerase activity
A0042732biological_processD-xylose metabolic process
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 391
ChainResidue
AGLU216
AHIS219
AASP254
AASP256
AHOH622

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 392
ChainResidue
AHOH588
AHOH627
AGLU180
AGLU216
AASP244
AASP286

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 393
ChainResidue
AALA200
AARG204
AGLN233

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
AASP54

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ALEU57

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING:
ChainResidueDetails
APRO181
AVAL217
AGLU220
ALEU245
AGLN255
ALEU257
APHE287

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
AASP254
ALYS182
AHIS219

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
AGLU180
ALYS182
AASP56
AHIS53

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon