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Crystal structure of 12-oxophytodienoate reductase 1 from tomato

Analyse Crystal structure of 12-oxophytodienoate reductase 1 from tomato in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ICS
Type: protein
Length: 706 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 12-oxophytodienoate reductase 1
EC: 1.3.1.42
UniProt: Q9XG54
Ligands: FMN
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	12-oxophytodienoate reductase 1 (EC 1.3.1.42)	protein	353	38% helix, 15% strand	Q9XG54

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B

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

Pockets

2 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	656	0.72	0.79	54	FMN
2	652	0.72	0.79	58	FMN

Compared structures

1ICS · Crystal structure of 12-oxophytodienoate reductase 1 from tomato · the same entry in another collection · chain A against A, TM-score 1.00
Q9XG54 · AlphaFold monomer V2.0 prediction for 12-oxophytodienoate reductase 1 (Q9XG54) · 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 Q9XG54
Elsewhere: RCSB PDB 1ICS · PDBe 1ICS · UniProt Q9XG54

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