1FYC

INNER LIPOYL DOMAIN FROM HUMAN PYRUVATE DEHYDROGENASE (PDH) COMPLEX, NMR, 1 STRUCTURE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006086	biological_process	pyruvate decarboxylation to acetyl-CoA
A	0045254	cellular_component	pyruvate dehydrogenase complex

Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	12
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PalSPtMTMGTV

Chain	Residue	Details
A	PRO15-VAL26

---

site_id	PS00189
Number of Residues	30
Details	LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GekLsegDLLaeIETdKATigFevqeeGyL

Chain	Residue	Details
A	GLY34-LEU63

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	76
Details	Domain: {"description":"Lipoyl-binding 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N6-lipoyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15861126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17532006","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17683942","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25525879","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Y8N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y8O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y8P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PNR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Q8I","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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