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Crystal structure of the bc domain of ACC2 in complex with soraphen a

Analyse Crystal structure of the bc domain of ACC2 in complex with soraphen a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3JRX
Type: protein
Length: 496 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyl-CoA carboxylase 2
EC: 6.4.1.2, 6.3.4.14
UniProt: O00763
Ligands: S1A
Pockets: 4 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyl-CoA carboxylase 2 (EC 6.4.1.2, 6.3.4.14)	protein	496	35% helix, 21% strand	O00763

Ligands and binding sites

S1A · Soraphen A · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1062	0.73	0.76	80	empty
2	371	0.66	0.79	47	S1A
3	184	0.48	0.75	31	empty
4	119	0.47	0.79	21	empty

Compared structures

3JRX · Crystal structure of the BC domain of ACC2 in complex with soraphen A · the same entry in another collection · chain A against A, TM-score 1.00
O00763 · AlphaFold monomer V2.0 prediction for acetyl-CoA carboxylase 2 (O00763) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 O00763
Elsewhere: RCSB PDB 3JRX · PDBe 3JRX · UniProt O00763

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