Research workbench
Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for ca-regulation
Analyse Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VF1
- Type
- protein
- Length
- 1,360 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 11R-lipoxygenase
- UniProt
- Q2N410
- Ligands
- GLC, FRU, FE2
- Pockets
- 13 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 11R-lipoxygenase | protein | 680 | 42% helix, 15% strand | Q2N410 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A, B
- FRU · beta-D-fructofuranose · sugar · 2 copies · chains A, 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
13 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 332 | 0.80 | 0.90 | 58 | empty |
| 2 | 325 | 0.78 | 0.89 | 58 | empty |
| 3 | 379 | 0.73 | 0.84 | 49 | empty |
| 4 | 666 | 0.71 | 0.78 | 56 | empty |
| 5 | 432 | 0.68 | 0.80 | 55 | empty |
Interfaces
1 interface between chains.
- A–B · 432 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3VF1 · Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca-regulation · 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 Q2N410
- Elsewhere: RCSB PDB 3VF1 · PDBe 3VF1 · UniProt Q2N410
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