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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 Residues20
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY75
BLYS148
CGLY75
CHIS82
CHIS88
CALA114
CLYS148
DGLY75
DHIS82
DHIS88
DALA114
AHIS82
DLYS148
AHIS88
AALA114
ALYS148
BGLY75
BHIS82
BHIS88
BALA114

site_idSWS_FT_FI2
Number of Residues12
DetailsSITE: Catalytically relevant
ChainResidueDetails
AALA59
DALA59
DGLU111
DGLU152
AGLU111
AGLU152
BALA59
BGLU111
BGLU152
CALA59
CGLU111
CGLU152

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PDB entries from 2024-07-24

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