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Crystal structure of (R)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and acetoacetate

Analyse Crystal structure of (R)-3-hydroxybutyrate dehydrogenase from acinetobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ZZQ
Type: protein
Length: 260 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-hydroxybutyrate dehydrogenase
UniProt: A0A1E3M3N6
Ligands: AAE, NAD
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-hydroxybutyrate dehydrogenase	protein	260	54% helix, 13% strand	A0A1E3M3N6

Ligands and binding sites

AAE · Acetoacetic acid · ligand · 2 copies · chains A
NAD · Nicotinamide-adenine-dinucleotide · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	354	0.71	0.83	37	NAD, AAE
2	74	0.35	0.76	14	empty

Compared structures

6ZZQ · Crystal structure of (R)-3-hydroxybutyrate dehydrogenase from Acinetobacter baumannii… · 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 A0A1E3M3N6
Elsewhere: RCSB PDB 6ZZQ · PDBe 6ZZQ · UniProt A0A1E3M3N6

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