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4J4K

Crystal structure 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 ZN A 401
ChainResidue
AGLU217
AHIS220
AASP255
AASP257
AHOH924

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
AHOH923
AGLU181
AGLU217
AASP245
AASP287

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 403
ChainResidue
AHIS49
AACT408
AHOH925

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 404
ChainResidue
AHIS71
AHOH909
AHOH910
AHOH911

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MPD A 405
ChainResidue
ATRP16
APRO25
APHE26
AHIS54
ATHR95
AHOH555
AHOH608
AHOH762

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD A 406
ChainResidue
ATRP16
AHIS54
APHE94
ATRP137
AASP287
AHOH597
AHOH790

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 407
ChainResidue
ALYS159
AARG205
ATRP237
AHOH840
AHOH860

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 408
ChainResidue
AARG10
ASER281
APRO283
AZN403
AHOH925

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

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PDB entries from 2025-06-18

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