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Bovine ACC2 ct domain in complex with inhibitor

Analyse Bovine ACC2 ct domain in complex with inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X24
Type: protein
Length: 1,321 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyl-CoA carboxylase
Ligands: X24
Pockets: 11 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyl-CoA carboxylase	protein	654	38% helix, 22% strand	—
B	Acetyl-CoA carboxylase	protein	667	39% helix, 21% strand	—

Ligands and binding sites

X24 · Tert-butyl [(trans-4-{[({2-[4-(aminomethyl)phenyl]quinolin-4-yl}carbonyl)amino]methyl}cyclohexyl)methyl]carbamate · ligand · 2 copies · chains A, B

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

Pockets

11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1020	0.84	0.85	101	X24
2	306	0.78	0.89	39	empty
3	500	0.77	0.84	54	X24
4	300	0.60	0.78	32	empty
5	230	0.55	0.77	33	empty

Interfaces

1 interface between chains.

A–B · 6163 Å² buried · 66 hydrogen bonds · protein-protein

Compared structures

2X24 · bovine ACC2 CT domain in complex with inhibitor · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 2X24 · PDBe 2X24

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