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Crystal structure of acetoacetyl-CoA reductase from burkholderia pseudomallei 1710B with bound NADP

Analyse Crystal structure of acetoacetyl-CoA reductase from burkholderia pseudomallei… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VML
Type: protein
Length: 245 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetoacetyl-CoA reductase
EC: 1.1.1.36
UniProt: Q3JRS9
Ligands: NAP
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetoacetyl-CoA reductase (EC 1.1.1.36)	protein	245	49% helix, 16% strand	Q3JRS9

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	511	0.67	0.78	48	NAP

Compared structures

5VML · Crystal Structure of Acetoacetyl-CoA Reductase from Burkholderia Pseudomallei 1710b with… · 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 Q3JRS9
Elsewhere: RCSB PDB 5VML · PDBe 5VML · UniProt Q3JRS9

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