Research workbench
Revised structure of rabbit reticulocyte 15S-lipoxygenase
Analyse Revised structure of rabbit reticulocyte 15S-lipoxygenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2P0M
- Type
- protein
- Length
- 1,324 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arachidonate 15-lipoxygenase
- EC
- 1.13.11.33
- UniProt
- P12530
- Ligands
- RS7, FE2
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Arachidonate 15-lipoxygenase (EC 1.13.11.33) | protein | 662 | 45% helix, 15% strand | P12530 |
Ligands and binding sites
- RS7 · (2E)-3-(2-oct-1-yn-1-ylphenyl)acrylic acid · ligand · chains B
- FE2 · Fe (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 266 | 0.84 | 0.96 | 34 | RS7 |
| 2 | 636 | 0.77 | 0.82 | 63 | empty |
| 3 | 585 | 0.76 | 0.82 | 55 | empty |
| 4 | 127 | 0.72 | 0.92 | 28 | empty |
| 5 | 271 | 0.67 | 0.83 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 1351 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2P0M · Revised structure of rabbit reticulocyte 15S-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 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 P12530
- Elsewhere: RCSB PDB 2P0M · PDBe 2P0M · UniProt P12530
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