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Three-dimensional structure of the lipoyl domain from bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex

Analyse Three-dimensional structure of the lipoyl domain from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LAB
Type: protein
Length: 80 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrolipoamide acetyltransferase
EC: 2.3.1.12
UniProt: P11961
Pockets: 1 · best druggability 0.59

Structure

solution nmr · 1 distinct chain · 0% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrolipoamide acetyltransferase (EC 2.3.1.12)	protein	80	0% helix, 30% strand	P11961

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	168	0.59	0.82	29	empty

Compared structures

1LAB · Three-dimensional structure of the lipoyl domain from bacillus stearothermophilus… · the same entry in another collection · chain A against A, TM-score 1.00
P11961 · AlphaFold monomer V2.0 prediction for dihydrolipoyllysine-residue acetyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.71

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P11961
Elsewhere: RCSB PDB 1LAB · PDBe 1LAB · UniProt P11961

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