MolNFT v1 · #121475 · protein

Mvas in complex with acetoacetyl coenzyme a

5HWQ · Hydroxymethylglutaryl-CoA synthase: “Mvas in complex with acetoacetyl coenzyme a”. X-ray diffraction, 2 ligands (CAA, SO4), 3 pockets (best druggability 0.69). MolNFT v1 #121475 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 5HWQ
Type: protein
Length: 418 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydroxymethylglutaryl-CoA synthase
EC: 2.3.3.10
UniProt: Q1D4I1
Ligands: CAA, SO4
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydroxymethylglutaryl-CoA synthase (EC 2.3.3.10)	protein	418	42% helix, 23% strand	Q1D4I1

Ligands and binding sites

CAA · Acetoacetyl-coenzyme A · ligand · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 4 copies · chains A

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

Pockets

3 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	396	0.69	0.82	54	empty
2	188	0.62	0.83	33	CAA
3	109	0.56	0.84	22	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

5HWQ · MvaS in complex with acetoacetyl coenzyme A · 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 Q1D4I1
Elsewhere: RCSB PDB 5HWQ · PDBe 5HWQ · UniProt Q1D4I1

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