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Crystal structure of lipoate-protein ligase a bound with lipoyl-AMP

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

PDB: 2ART
Type: protein
Length: 247 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: LPA, AMP, MG
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipoate-protein ligase a (EC 6.3.2.-)	protein	247	35% helix, 26% strand	Q9HKT1

Ligands and binding sites

LPA · Lipoic acid · ligand · chains A
AMP · Adenosine monophosphate · ligand · chains A
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	407	0.75	0.85	59	MG, LPA, AMP

Compared structures

2ART · Crystal structure of lipoate-protein ligase A bound with lipoyl-AMP · 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 2ART · PDBe 2ART · UniProt Q9HKT1

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