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X-ray crystal structure of a double bond reductase from nicotiana tabacum

Analyse X-ray crystal structure of a double bond reductase from nicotiana tabacum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HFJ
Type: protein
Length: 659 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Allyl alcohol dehydrogenase
EC: 1.3.1.74
UniProt: Q9SLN8
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Allyl alcohol dehydrogenase (EC 1.3.1.74)	protein	333	32% helix, 30% strand	Q9SLN8
B	Allyl alcohol dehydrogenase (EC 1.3.1.74)	protein	326	32% helix, 30% strand	Q9SLN8

Pockets

3 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	570	0.78	0.84	58	empty
2	706	0.71	0.78	58	empty
3	130	0.46	0.77	29	empty

Interfaces

1 interface between chains.

A–B · 1058 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

4HFJ · X-ray Crystal Structure of a Double Bond Reductase from Nicotiana tabacum · the same entry in another collection · chain A against A, TM-score 1.00
Q9SLN8 · AlphaFold monomer V2.0 prediction for 2-alkenal reductase (NADP(+)-dependent) (Q9SLN8) · a predicted model of the same protein · chain A 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 Q9SLN8
Elsewhere: RCSB PDB 4HFJ · PDBe 4HFJ · UniProt Q9SLN8

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