MolNFT v1 · #84212 · protein
D11-C mutant of monoamine oxidase from aspergillus niger
3ZDN · Monoamine oxidase N: “D11-C mutant of monoamine oxidase from aspergillus niger”. X-ray diffraction, 1 ligand (FAD), 20 pockets (best druggability 0.87). MolNFT v1 #84212 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3ZDN
- Type
- protein
- Length
- 1,907 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Monoamine oxidase N
- EC
- 1.4.3.4
- UniProt
- P46882
- Ligands
- FAD
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 4 distinct chains · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Monoamine oxidase N (EC 1.4.3.4) | protein | 478 | 34% helix, 23% strand | P46882 |
| B | Monoamine oxidase N (EC 1.4.3.4) | protein | 476 | 32% helix, 24% strand | P46882 |
| C | Monoamine oxidase N (EC 1.4.3.4) | protein | 477 | 34% helix, 23% strand | P46882 |
| D | Monoamine oxidase N (EC 1.4.3.4) | protein | 476 | 34% helix, 23% strand | P46882 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 815 | 0.87 | 0.89 | 101 | FAD |
| 2 | 816 | 0.87 | 0.89 | 94 | FAD |
| 3 | 818 | 0.87 | 0.89 | 99 | FAD |
| 4 | 817 | 0.86 | 0.88 | 98 | FAD |
| 5 | 104 | 0.76 | 0.97 | 25 | empty |
Interfaces
4 interfaces between chains.
- C–D · 1760 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1722 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 306 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 304 Ų buried · 6 hydrogen bonds · protein-protein
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 P46882
- Elsewhere: RCSB PDB 3ZDN · PDBe 3ZDN · UniProt P46882
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.