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Crystal structure of the biotin carboxylase subunit, E23R mutant, of acetyl-CoA carboxylase from escherichia COLI.

Analyse Crystal structure of the biotin carboxylase subunit, E23R mutant, of acetyl-CoA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2GPS
Type
protein
Length
893 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Biotin carboxylase
EC
6.3.4.14
UniProt
P24182
Pockets
9 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABiotin carboxylase (EC 6.3.4.14)protein44734% helix, 23% strandP24182
BBiotin carboxylase (EC 6.3.4.14)protein44635% helix, 27% strandP24182

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15850.750.8255empty
2640.690.9621empty
32910.540.7535empty
42000.490.7624empty
51180.440.7822empty

Interfaces

1 interface between chains.

  • A–B · 1338 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 2GPS · Crystal Structure of the Biotin Carboxylase Subunit, E23R mutant, of Acetyl-CoA… · the same entry in another collection · chain A against A, TM-score 1.00
  • P24182 · AlphaFold monomer V2.0 prediction for biotin carboxylase (P24182) · a predicted model of the same protein · chain B against A, TM-score 0.91

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