MolNFT v1 · #36557 · protein

Hmg-CoA synthase from brassica juncea in complex with F-244

2F9A · 3-hydroxy-3-methylglutaryl coenzyme a synthase 1: “Hmg-CoA synthase from brassica juncea in complex with F-244”. X-ray diffraction, 1 ligand (F24), 2 pockets (best druggability 0.77). MolNFT v1 #36557 on GenesisL1: 3D structure…

PDB: 2F9A
Type: protein
Length: 404 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-hydroxy-3-methylglutaryl coenzyme a synthase 1
UniProt: Q9M6U3
Ligands: F24
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-hydroxy-3-methylglutaryl coenzyme a synthase 1	protein	404	38% helix, 24% strand	Q9M6U3

Ligands and binding sites

F24 · (7R,12R,13R)-13-formyl-12,14-dihydroxy-3,5,7-trimethyltetradeca-2,4-dienoic acid · ligand · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	689	0.77	0.82	73	F24
2	155	0.53	0.80	25	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

2F9A · HMG-CoA synthase from Brassica juncea in complex with F-244 · 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 2F9A · PDBe 2F9A · UniProt Q9M6U3

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