Research workbench
Manganese-substituted cyanothece lipoxygenase 2 (mn-CSPLOX2)
Analyse Manganese-substituted cyanothece lipoxygenase 2 (mn-CSPLOX2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MEG
- Type
- protein
- Length
- 1,132 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
- B7JX99
- Ligands
- MN, CL
- Pockets
- 16 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arachidonate 15-lipoxygenase (EC 1.13.11.33) | protein | 569 | 52% helix, 9% strand | B7JX99 |
| B | Arachidonate 15-lipoxygenase (EC 1.13.11.33) | protein | 563 | 53% helix, 10% strand | B7JX99 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A
- EOH · Ethanol · additive · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 304 | 0.66 | 0.82 | 34 | EOH |
| 2 | 283 | 0.65 | 0.81 | 51 | EOH |
| 3 | 299 | 0.65 | 0.81 | 31 | empty |
| 4 | 255 | 0.64 | 0.82 | 49 | EOH |
| 5 | 312 | 0.59 | 0.77 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 1462 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 5MEG · Manganese-substituted Cyanothece lipoxygenase 2 (Mn-CspLOX2) · the same entry in another collection · 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 B7JX99
- Elsewhere: RCSB PDB 5MEG · PDBe 5MEG · UniProt B7JX99
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