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2XHZ

Probing the active site of the sugar isomerase domain from E. coli arabinose-5-phosphate isomerase via X-ray crystallography

Functional Information from GO Data
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0016853molecular_functionisomerase activity
A0097367molecular_functioncarbohydrate derivative binding
A1901135biological_processcarbohydrate derivative metabolic process
B0005975biological_processcarbohydrate metabolic process
B0016853molecular_functionisomerase activity
B0097367molecular_functioncarbohydrate derivative binding
B1901135biological_processcarbohydrate derivative metabolic process
C0005975biological_processcarbohydrate metabolic process
C0016853molecular_functionisomerase activity
C0097367molecular_functioncarbohydrate derivative binding
C1901135biological_processcarbohydrate derivative metabolic process
D0005975biological_processcarbohydrate metabolic process
D0016853molecular_functionisomerase activity
D0097367molecular_functioncarbohydrate derivative binding
D1901135biological_processcarbohydrate derivative metabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues56
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsSite: {"description":"Catalytically relevant"}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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