1IYU

LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004742	molecular_function	dihydrolipoyllysine-residue acetyltransferase activity
A	0006096	biological_process	glycolytic process
A	0045254	cellular_component	pyruvate dehydrogenase complex

Functional Information from PDB Data

site_id	LIP
Number of Residues	1
Details	LYS 39 IS THE LIPOYLATION SITE WHERE LIPOIC ACID (6,8 THIOCTIC ACID) IS COVALENTLY ATTACHED VIA AN AMIDE LINKAGE TO THE LYSINE SIDE CHAIN.

Chain	Residue
A	LYS39

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY23-VAL52

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	72
Details	Domain: {"description":"Lipoyl-binding 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N6-lipoyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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