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Crystal structure of lipoate-protein ligase a from thermoplasma acidophilum

Analyse Crystal structure of lipoate-protein ligase a from thermoplasma acidophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ARS
Type: protein
Length: 245 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipoate-protein ligase a
EC: 6.3.2.-
UniProt: Q9HKT1
Ligands: MG
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipoate-protein ligase a (EC 6.3.2.-)	protein	245	37% helix, 27% strand	Q9HKT1

Ligands and binding sites

MG · Magnesium ion · metal · chains A

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

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	349	0.72	0.84	56	MG

Modifications

Observed in the structure: 13 modified (engineered).

Compared structures

2ARS · Crystal structure of lipoate-protein ligase A From Thermoplasma acidophilum · the same entry in another collection · chain A against A, TM-score 1.00
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 0.96

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
Elsewhere: RCSB PDB 2ARS · PDBe 2ARS · UniProt Q9HKT1

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