Research workbench

L-3-hydroxyacyl-CoA dehydrogenase (apo)

Analyse L-3-hydroxyacyl-CoA dehydrogenase (apo) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1F14
Type: protein
Length: 582 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-3-hydroxyacyl-CoA dehydrogenase
EC: 1.1.1.35
UniProt: Q16836
Pockets: 9 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	L-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)	protein	291	52% helix, 14% strand	Q16836

Pockets

9 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	513	0.69	0.79	61	empty
2	410	0.68	0.80	44	empty
3	70	0.44	0.81	20	empty
4	117	0.43	0.77	26	empty
5	71	0.39	0.79	17	empty

Interfaces

1 interface between chains.

A–B · 1646 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

1F14 · L-3-hydroxyacyl-CoA dehydrogenase (apo) · the same entry in another collection · chain A against A, TM-score 1.00
Q16836 · AlphaFold monomer V2.0 prediction for hydroxyacyl-coenzyme a dehydrogenase, mitochondrial… · a predicted model of the same protein · 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 Q16836
Elsewhere: RCSB PDB 1F14 · PDBe 1F14 · UniProt Q16836

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