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Crystal Structure of Biotin Carboxylase from Haemophilus influenzae in Complex with ADP and Phosphate

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
4MV1
Type
protein
Length
430 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.91
Source
Haemophilus influenzae
Molecule
Biotin carboxylase
EC
6.3.4.14, 6.4.1.2
UniProt
P43873
Ligands
ADP, PO4
Pockets
1 · best druggability 0.68

Structure

x-ray diffraction · resolution 1.91 · 1 distinct chain · 37% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABiotin carboxylase (EC 6.3.4.14, 6.4.1.2)protein43037% helix, 27% strandP43873

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • PO4 · Phosphate ion · ion · chains A
  • EDO · 1,2-ethanediol · additive · 2 copies · 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
15900.680.7754PO4, ADP

Compared structures

  • 4MV1 · Crystal structure of biotin carboxylase from haemophilus influenzae in complex with ADP… · 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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