MolNFT v1 · #36581 · protein

Hmg-CoA synthase from brassica juncea in complex with hmg-CoA and covalently bound to hmg-CoA

2FA0: “Hmg-CoA synthase from brassica juncea in complex with hmg-CoA and covalently bound to hmg-CoA”. X-ray diffraction, 1 ligand (HMG), 6 pockets (best druggability 0.66). MolNFT v1 #36581 on GenesisL1: 3D structure, binding sites and…

PDB: 2FA0
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: HMG
Pockets: 6 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hmg-CoA synthase	protein	450	44% helix, 22% strand	Q9M6U3

Ligands and binding sites

HMG · 3-hydroxy-3-methylglutaryl-coenzyme A · ligand · chains A

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

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	127	0.66	0.88	29	empty
2	183	0.62	0.83	27	HMG
3	63	0.52	0.86	18	empty
4	167	0.51	0.79	28	empty
5	115	0.43	0.77	19	empty

Modifications

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

Compared structures

2FA0 · HMG-CoA synthase from Brassica juncea in complex with HMG-CoA and covalently bound to… · 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 2FA0 · PDBe 2FA0 · UniProt Q9M6U3

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