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The structure of salutaridine reductase from papaver somniferum.

Analyse The structure of salutaridine reductase from papaver somniferum. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3O26
Type: protein
Length: 294 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Salutaridine reductase
EC: 1.1.1.248
UniProt: Q071N0
Ligands: NDP
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Salutaridine reductase (EC 1.1.1.248)	protein	294	52% helix, 13% strand	Q071N0

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · 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	698	0.76	0.81	55	NDP
2	52	0.33	0.78	14	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3O26 · The structure of salutaridine reductase from Papaver somniferum. · the same entry in another collection · chain A against A, TM-score 1.00
Q071N0 · AlphaFold monomer V2.0 prediction for salutaridine reductase (Q071N0) · 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 Q071N0
Elsewhere: RCSB PDB 3O26 · PDBe 3O26 · UniProt Q071N0

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