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The structure of biotin carboxylase, mutant E288K, complexed with ATP

Analyse The structure of biotin carboxylase, mutant E288K, complexed with ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1DV2
Type: protein
Length: 898 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
Ligands: ATP
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Biotin carboxylase (EC 6.3.4.14)	protein	450	36% helix, 27% strand	P24182
B	Biotin carboxylase (EC 6.3.4.14)	protein	448	34% helix, 27% strand	P24182

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	523	0.76	0.83	53	empty
2	819	0.73	0.78	70	ATP
3	849	0.73	0.78	67	ATP
4	77	0.71	0.96	30	empty
5	66	0.35	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 1284 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

1DV2 · The structure of biotin carboxylase, mutant E288K, complexed with ATP · 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 0.99

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 P24182
Elsewhere: RCSB PDB 1DV2 · PDBe 1DV2 · UniProt P24182

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