Hmg-CoA reductase from pseudomonas mevalonii complexed with NAD and intermediate hemiacetal form of hmg-CoA

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 21% strand (DSSP).

Ligands and binding sites

• 1CV · (3R,5R,9R,19R,21S)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9,21-tetrahydroxy-8,8,21-trimethyl-10,14-dioxo-19-sulfanyl-2,4,6-trioxa-18-thia-11,15-diaza-3,5-diphosphatricosan-23-oic acid 3,5-dioxide · ligand · chains A, B
• NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A, B
• 1CO · (3S)-3-hydroxy-3-methyl-5-sulfanylpentanoic acid · ligand · chains A, B
• SO4 · Sulfate ion · ion · chains A
• GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 5569 Ų buried · 98 hydrogen bonds · protein-protein

Compared structures

• 4I4B · HMG-CoA Reductase from Pseudomonas mevalonii complexed with NAD and intermediate… · the same entry in another collection · chain B against B, TM-score 1.00
• P13702 · AlphaFold monomer V2.0 prediction for 3-hydroxy-3-methylglutaryl- coenzyme a reductase… · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P13702
• Elsewhere: RCSB PDB 4I4B · PDBe 4I4B · UniProt P13702