Research workbench

Rabbit reticulocyte 15-lipoxygenase

Analyse Rabbit reticulocyte 15-lipoxygenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LOX
Type: protein
Length: 647 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 15-lipoxygenase
EC: 1.13.11.33
UniProt: P12530
Ligands: RS7, FE2
Pockets: 7 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	15-lipoxygenase (EC 1.13.11.33)	protein	647	44% helix, 15% strand	P12530

Ligands and binding sites

RS7 · (2E)-3-(2-oct-1-yn-1-ylphenyl)acrylic acid · ligand · chains A
FE2 · Fe (II) ion · metal · chains A

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	831	0.78	0.81	88	empty
2	164	0.71	0.89	27	RS7
3	278	0.60	0.79	25	empty
4	87	0.41	0.78	17	empty
5	64	0.31	0.75	12	empty

Compared structures

1LOX · Rabbit reticulocyte 15-lipoxygenase · the same entry in another collection · chain A against A, TM-score 1.00
P12530 · AlphaFold monomer V2.0 prediction for polyunsaturated fatty acid lipoxygenase ALOX15… · 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 P12530
Elsewhere: RCSB PDB 1LOX · PDBe 1LOX · UniProt P12530

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