MolNFT v1 · #68871 · protein

Crystal structure of the carboxyltransferase domain of acetyl-coenzyme a carboxylase in complex with tepraloxydim

3K8X · Acetyl-CoA carboxylase: “Crystal structure of the carboxyltransferase domain of acetyl-coenzyme a carboxylase in complex with…”. X-ray diffraction, 1 ligand (B89), 20 pockets (best druggability 0.81). MolNFT v1 #68871 on GenesisL1…

PDB: 3K8X
Type: protein
Length: 2,045 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyl-CoA carboxylase
EC: 6.4.1.2, 6.3.4.14
UniProt: Q00955
Ligands: B89
Pockets: 20 · best druggability 0.81

Structure

x-ray diffraction · 3 distinct chains · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14)	protein	688	39% helix, 21% strand	Q00955
B	Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14)	protein	682	39% helix, 21% strand	Q00955
C	Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14)	protein	675	40% helix, 21% strand	Q00955

Ligands and binding sites

B89 · (5S)-2-[(1E)-N-{[(2E)-3-chloroprop-2-en-1-yl]oxy}propanimidoyl]-3-hydroxy-5-(tetrahydro-2H-pyran-4-yl)cyclohex-2-en-1-one · ligand · 3 copies · chains A, B, C

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

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	813	0.81	0.84	59	empty
2	648	0.76	0.82	62	B89
3	495	0.76	0.84	33	empty
4	446	0.74	0.83	52	B89
5	519	0.71	0.80	33	empty

Interfaces

2 interfaces between chains.

B–C · 5871 Å² buried · 39 hydrogen bonds · protein-protein
A–B · 1354 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

3K8X · Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase in… · the same entry in another collection · chain A against A, TM-score 1.00
Q00955 · AlphaFold monomer V2.0 prediction for acetyl-CoA carboxylase (Q00955) · a predicted model of the same protein · chain C against A, TM-score 0.99

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 Q00955
Elsewhere: RCSB PDB 3K8X · PDBe 3K8X · UniProt Q00955

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