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3UWY

Crystal structure of triosephosphate isomerase from Methicillin resistant Staphylococcus Aureus at 2.4 angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0019563biological_processglycerol catabolic process
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
B0004807molecular_functiontriose-phosphate isomerase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0019563biological_processglycerol catabolic process
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPIWAIGTG
ChainResidueDetails
AALA167-GLY177

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Electrophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00147","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22813930","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00147","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22813930","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00147","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22813930","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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