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Crystal structure of domains AC1-AC2 of yeast acetyl-CoA carboxylase

Analyse Crystal structure of domains AC1-AC2 of yeast acetyl-CoA carboxylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CS0
Type: protein
Length: 423 residues
Chains: 2
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
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14)	protein	215	80% helix, 0% strand	Q00955
B	Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14)	protein	208	80% helix, 0% strand	Q00955

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	662	0.71	0.78	67	empty

Interfaces

1 interface between chains.

A–B · 2275 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

5CS0 · Crystal structure of domains AC1-AC2 of yeast acetyl-CoA carboxylase · 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 A against A, TM-score 0.90

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 5CS0 · PDBe 5CS0 · UniProt Q00955

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