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1SCZ

Improved structural model for the catalytic domain of E.coli dihydrolipoamide succinyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004149molecular_functiondihydrolipoyllysine-residue succinyltransferase activity
A0006099biological_processtricarboxylic acid cycle
A0016746molecular_functionacyltransferase activity
A0045252cellular_componentoxoglutarate dehydrogenase complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"10739245","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9677295","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 704
ChainResidueDetails
ATHR323electrostatic stabiliser, polar interaction
AHIS375activator, proton acceptor, proton donor

246704

PDB entries from 2025-12-24

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