Research workbench
Pseudooxynicotine amine oxidase
Analyse Pseudooxynicotine amine oxidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7U6L
- Type
- protein
- Length
- 1,740 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amine oxidase
- UniProt
- F8G0P1
- Ligands
- FAD
- Pockets
- 16 · best druggability 0.86
Structure
x-ray diffraction · 4 distinct chains · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amine oxidase | protein | 434 | 36% helix, 23% strand | F8G0P1 |
| B | Amine oxidase | protein | 435 | 37% helix, 23% strand | F8G0P1 |
| C | Amine oxidase | protein | 435 | 36% helix, 23% strand | F8G0P1 |
| D | Amine oxidase | protein | 436 | 37% helix, 23% strand | F8G0P1 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 434 | 0.86 | 0.94 | 68 | FAD |
| 2 | 467 | 0.86 | 0.93 | 74 | FAD |
| 3 | 462 | 0.85 | 0.92 | 70 | FAD |
| 4 | 697 | 0.84 | 0.88 | 98 | FAD |
| 5 | 225 | 0.55 | 0.78 | 32 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1477 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 366 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 61 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7U6L · Pseudooxynicotine amine oxidase · 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 F8G0P1
- Elsewhere: RCSB PDB 7U6L · PDBe 7U6L · UniProt F8G0P1
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