MolNFT v1 · #77377 · protein

Crystal structure of acyl-CoA thioesterase from mycobacterium avium

3RD7: “Crystal structure of acyl-CoA thioesterase from mycobacterium avium”. X-ray diffraction, 1 ligand (CL), 5 pockets (best druggability 0.76). MolNFT v1 #77377 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3RD7
Type: protein
Length: 551 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acyl-CoA thioesterase
UniProt: A0QFP4
Ligands: CL
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acyl-CoA thioesterase	protein	275	21% helix, 40% strand	A0QFP4
B	Acyl-CoA thioesterase	protein	276	22% helix, 39% strand	A0QFP4

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	777	0.76	0.80	61	CL
2	789	0.73	0.77	71	CL
3	177	0.55	0.79	32	empty
4	129	0.52	0.81	24	empty
5	125	0.51	0.80	21	empty

Interfaces

1 interface between chains.

A–B · 2431 Å² buried · 46 hydrogen bonds · protein-protein

Compared structures

3RD7 · Crystal structure of acyl-coa thioesterase from mycobacterium avium · 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 A0QFP4
Elsewhere: RCSB PDB 3RD7 · PDBe 3RD7 · UniProt A0QFP4

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