MolNFT v1 · #115737 · protein

Crystal structure of yeast acetyl-CoA carboxylase, unbiotinylated

5CSK: “Crystal structure of yeast acetyl-CoA carboxylase, unbiotinylated”. X-ray diffraction, 20 pockets (best druggability 0.87). MolNFT v1 #115737 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5CSK
Type: protein
Length: 4,013 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: 20 · best druggability 0.87

Structure

x-ray diffraction · 2 distinct chains · 40% 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	1996	41% helix, 21% strand	Q00955
B	Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14)	protein	2017	40% helix, 20% strand	Q00955

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	641	0.87	0.91	75	empty
2	633	0.86	0.91	81	empty
3	871	0.84	0.86	85	empty
4	205	0.81	0.94	35	empty
5	795	0.79	0.83	72	empty

Interfaces

1 interface between chains.

A–B · 9264 Å² buried · 106 hydrogen bonds · protein-protein

Compared structures

Q00955 · AlphaFold monomer V2.0 prediction for acetyl-CoA carboxylase (Q00955) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 5CSK · PDBe 5CSK · UniProt Q00955

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