Research workbench

Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase

Analyse Structure and function of a single-chain, multi-domain long-chain acyl-CoA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RCN
Type: protein
Length: 1,972 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Long-chain acyl-CoA carboxylase
UniProt: Q73VY8
Pockets: 20 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Long-chain acyl-CoA carboxylase	protein	972	33% helix, 25% strand	Q73VY8
B	Long-chain acyl-CoA carboxylase	protein	1000	33% helix, 25% strand	Q73VY8

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	560	0.75	0.83	48	empty
2	595	0.70	0.79	55	empty
3	425	0.69	0.81	59	empty
4	373	0.67	0.81	54	empty
5	286	0.57	0.77	40	empty

Interfaces

1 interface between chains.

A–B · 1989 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

4RCN · Structure and function of a single-chain, multi-domain long-chain acyl-coa 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 Q73VY8
Elsewhere: RCSB PDB 4RCN · PDBe 4RCN · UniProt Q73VY8

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.