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Lipoxygenase-3(SOYBEAN) non-heme FE(II) metalloprotein

Analyse Lipoxygenase-3(SOYBEAN) non-heme FE(II) metalloprotein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LNH
Type: protein
Length: 836 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipoxygenase-3
UniProt: P09186
Ligands: FE2
Pockets: 10 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipoxygenase-3	protein	836	39% helix, 14% strand	P09186

Ligands and binding sites

FE2 · Fe (II) ion · metal · chains A

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

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	648	0.81	0.86	65	empty
2	63	0.72	0.98	20	empty
3	418	0.71	0.82	35	empty
4	501	0.70	0.80	43	empty
5	50	0.70	0.98	18	empty

Compared structures

1LNH · Lipoxygenase-3(SOYBEAN) non-heme FE(II) metalloprotein · the same entry in another collection · chain A against A, TM-score 1.00
P09186 · AlphaFold monomer V2.0 prediction for seed linoleate 9S-lipoxygenase-3 (P09186) · 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 P09186
Elsewhere: RCSB PDB 1LNH · PDBe 1LNH · UniProt P09186

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