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Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate

Analyse Crystal structure of biotin carboxylase from haemophilus influenzae in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4MV3
Type
protein
Length
439 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Biotin carboxylase
EC
6.3.4.14, 6.4.1.2
UniProt
P43873
Ligands
ACP, BCT
Pockets
1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABiotin carboxylase (EC 6.3.4.14, 6.4.1.2)protein43937% helix, 27% strandP43873

Ligands and binding sites

  • ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains A
  • BCT · Bicarbonate ion · ligand · chains A
  • EDO · 1,2-ethanediol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14590.640.7749ACP, BCT

Compared structures

  • 4MV3 · Crystal Structure of Biotin Carboxylase from Haemophilus influenzae in Complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • P43873 · AlphaFold monomer V2.0 prediction for biotin carboxylase (P43873) · a predicted model of the same protein · chain A against A, TM-score 0.99

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