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Propionyl-CoA carboxylase beta subunit, D422V

Analyse Propionyl-CoA carboxylase beta subunit, D422V in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IAV
Type: protein
Length: 1,042 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Propionyl-CoA carboxylase complex B subunit
UniProt: Q9X4K7
Ligands: SO4
Pockets: 13 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Propionyl-CoA carboxylase complex B subunit	protein	521	43% helix, 18% strand	Q9X4K7

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A, B

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

Pockets

13 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	54	0.70	0.98	23	empty
2	51	0.70	0.98	21	empty
3	615	0.67	0.76	59	SO4
4	479	0.65	0.77	48	SO4
5	294	0.65	0.81	52	empty

Interfaces

1 interface between chains.

A–B · 4757 Å² buried · 54 hydrogen bonds · protein-protein

Compared structures

3IAV · Propionyl-CoA Carboxylase Beta Subunit, D422V · 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 Q9X4K7
Elsewhere: RCSB PDB 3IAV · PDBe 3IAV · UniProt Q9X4K7

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