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Acyl-CoA carboxylase beta subunit from S. coelicolor (pccb), apo form #1

Analyse Acyl-CoA carboxylase beta subunit from S. coelicolor (pccb), apo form #1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XNV
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
EC: 6.4.1.3
UniProt: Q9X4K7
Pockets: 13 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Propionyl-CoA carboxylase complex B subunit (EC 6.4.1.3)	protein	521	45% helix, 18% strand	Q9X4K7

Pockets

13 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	568	0.68	0.77	59	empty
2	537	0.67	0.78	55	empty
3	154	0.52	0.79	29	empty
4	59	0.49	0.85	23	empty
5	61	0.43	0.82	21	empty

Interfaces

1 interface between chains.

A–B · 4793 Å² buried · 67 hydrogen bonds · protein-protein

Compared structures

1XNV · Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB), apo form #1 · 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 1XNV · PDBe 1XNV · UniProt Q9X4K7

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