MolNFT v1 · #182668 · protein

Structural basis for branched substrate selectivity in a ketoreductase from ascaris suum

7N09 · 3-hydroxyacyl-CoA dehydrogenase type-2: “Structural basis for branched substrate selectivity in a ketoreductase from ascaris suum”. X-ray diffraction, 1 ligand (NAD), 4 pockets (best druggability 0.74). MolNFT v1 #182668 on…

PDB: 7N09
Type: protein
Length: 518 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-hydroxyacyl-CoA dehydrogenase type-2
UniProt: F1L0H2
Ligands: NAD
Pockets: 4 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	3-hydroxyacyl-CoA dehydrogenase type-2	protein	259	44% helix, 17% strand	F1L0H2

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	438	0.74	0.83	47	NAD
2	412	0.72	0.83	47	NAD
3	90	0.43	0.79	21	empty
4	99	0.34	0.73	18	empty

Interfaces

1 interface between chains.

A–B · 1809 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

7N09 · Structural basis for branched substrate selectivity in a ketoreductase from Ascaris suum · 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 F1L0H2
Elsewhere: RCSB PDB 7N09 · PDBe 7N09 · UniProt F1L0H2

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