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Crystal structure of the biotin carboxylase domain of pyruvate carboxylase

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

PDB: 2DZD
Type: protein
Length: 912 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyruvate carboxylase
EC: 6.4.1.1
UniProt: Q05FZ3
Pockets: 9 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pyruvate carboxylase (EC 6.4.1.1)	protein	459	36% helix, 25% strand	Q05FZ3
B	Pyruvate carboxylase (EC 6.4.1.1)	protein	453	35% helix, 26% strand	Q05FZ3

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	991	0.83	0.85	92	empty
2	124	0.68	0.90	33	empty
3	478	0.60	0.75	44	empty
4	320	0.57	0.76	35	empty
5	325	0.57	0.76	35	empty

Interfaces

1 interface between chains.

A–B · 1384 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

2DZD · Crystal structure of the biotin carboxylase domain of pyruvate carboxylase · the same entry in another collection · chain A against A, TM-score 1.00

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 Q05FZ3
Elsewhere: RCSB PDB 2DZD · PDBe 2DZD · UniProt Q05FZ3

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