Research workbench
Manganese lipoxygenase
Analyse Manganese lipoxygenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FNO
- Type
- protein
- Length
- 1,136 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Manganese lipoxygenase
- EC
- 1.13.11.45
- UniProt
- G4NAP4
- Ligands
- NAG, MN
- Pockets
- 15 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Manganese lipoxygenase (EC 1.13.11.45) | protein | 568 | 52% helix, 6% strand | G4NAP4 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1109 | 0.87 | 0.88 | 127 | empty |
| 2 | 169 | 0.78 | 0.94 | 31 | empty |
| 3 | 179 | 0.75 | 0.91 | 33 | empty |
| 4 | 108 | 0.67 | 0.90 | 26 | empty |
| 5 | 120 | 0.66 | 0.89 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1323 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 glycan (N-glycosylation, glycosylation).
Compared structures
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 G4NAP4
- Elsewhere: RCSB PDB 5FNO · PDBe 5FNO · UniProt G4NAP4
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