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Crystal structure of domains bt-bccp-AC1-AC5 of yeast acetyl-CoA carboxylase

Analyse Crystal structure of domains bt-bccp-AC1-AC5 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
5CSA
Type
protein
Length
1,724 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 0.80

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAcetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14)protein87240% helix, 23% strandQ00955
BAcetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14)protein85239% helix, 23% strandQ00955

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11800.800.9532empty
26710.700.7867empty
33990.660.7944empty
45310.650.7641empty
53220.610.7851empty

Interfaces

1 interface between chains.

  • A–B · 2119 Ų buried · 27 hydrogen bonds · protein-protein

Compared structures

  • 5CSA · Crystal structure of domains BT-BCCP-AC1-AC5 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 B against A, TM-score 0.67

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