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3P14

Crystal structure of L-rhamnose isomerase with a novel high thermo-stability from Bacillus halodurans

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0008740molecular_functionL-rhamnose isomerase activity
A0019301biological_processrhamnose catabolic process
A0019324biological_processL-lyxose metabolic process
A0030145molecular_functionmanganese ion binding
B0005737cellular_componentcytoplasm
B0008740molecular_functionL-rhamnose isomerase activity
B0019301biological_processrhamnose catabolic process
B0019324biological_processL-lyxose metabolic process
B0030145molecular_functionmanganese ion binding
C0005737cellular_componentcytoplasm
C0008740molecular_functionL-rhamnose isomerase activity
C0019301biological_processrhamnose catabolic process
C0019324biological_processL-lyxose metabolic process
C0030145molecular_functionmanganese ion binding
D0005737cellular_componentcytoplasm
D0008740molecular_functionL-rhamnose isomerase activity
D0019301biological_processrhamnose catabolic process
D0019324biological_processL-lyxose metabolic process
D0030145molecular_functionmanganese ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2026-05-06

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