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Hmg-CoA synthase from brassica juncea in complex with acetyl-CoA and acetyl-CYS117.

Analyse Hmg-CoA synthase from brassica juncea in complex with acetyl-CoA and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FA3
Type: protein
Length: 450 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hmg-CoA synthase
UniProt: Q9M6U3
Ligands: ACO
Pockets: 5 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hmg-CoA synthase	protein	450	41% helix, 21% strand	Q9M6U3

Ligands and binding sites

ACO · Acetyl coenzyme *A · ligand · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	144	0.74	0.92	37	empty
2	178	0.61	0.83	21	empty
3	159	0.54	0.80	26	empty
4	118	0.42	0.76	22	empty
5	52	0.36	0.80	17	empty

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

2FA3 · HMG-CoA synthase from Brassica juncea in complex with acetyl-CoA and acetyl-cys117. · 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 Q9M6U3
Elsewhere: RCSB PDB 2FA3 · PDBe 2FA3 · UniProt Q9M6U3

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