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Crystal structure of biotin carboxylase from haemophilus influenzae in complex with phosphonoacetamide

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: 4MV6
Type: protein
Length: 412 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: PCT
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Biotin carboxylase (EC 6.3.4.14, 6.4.1.2)	protein	412	35% helix, 27% strand	P43873

Ligands and binding sites

PCT · Phosphonoacetamide · ligand · chains A
EDO · 1,2-ethanediol · additive · 3 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	424	0.61	0.76	50	PCT

Compared structures

4MV6 · 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

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 P43873
Elsewhere: RCSB PDB 4MV6 · PDBe 4MV6 · UniProt P43873

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