Structural analysis of an archaeal lipoylation system. a bi-partite lipoate protein ligase and its E2 lipoyl domain from thermoplasma acidophilum

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 29% strand (DSSP).

Ligands and binding sites

• MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A
• ACT · Acetate ion · additive · 2 copies · chains A, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Interfaces

1 interface between chains.

• A–C · 838 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

• 3R07 · Structural analysis of an archaeal lipoylation system. A bi-partite lipoate protein… · the same entry in another collection · chain A against A, TM-score 1.00
• Q9HKT2 · AlphaFold monomer V2.0 prediction for lipoate-protein ligase a subunit 2 (Q9HKT2) · a predicted model of the same protein · chain C against A, TM-score 0.99
• Q9HKT1 · AlphaFold monomer V2.0 prediction for lipoate-protein ligase a subunit 1 (Q9HKT1) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q9HKT1
• Every structure of UniProt Q9HKT2
• Elsewhere: RCSB PDB 3R07 · PDBe 3R07 · UniProt Q9HKT1 · UniProt Q9HKT2