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6OQZ

Crystal structure of Glucose Isomerase from Non-merohedrally twinned crystals

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 MN A 401
ChainResidue
AGLU217
AHIS220
AASP255
AASP257
AHOH636

site_idAC2
Number of Residues6
Detailsbinding site for residue MN A 402
ChainResidue
AMPD404
AHOH504
AGLU181
AGLU217
AASP245
AASP287

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 403
ChainResidue
AGLU181
AGLU217
AASP245
AASP287
AMPD404
AHOH504

site_idAC4
Number of Residues10
Detailsbinding site for residue MPD A 404
ChainResidue
ATRP16
AHIS54
ATHR90
ATRP137
AGLU181
AASP287
AMN402
AMG403
AHOH537
AHOH598

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
AHIS54

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AASP57

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING:
ChainResidueDetails
AGLU181
AGLU217
AHIS220
AASP245
AASP255
AASP257
AASP287

219140

PDB entries from 2024-05-01

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