Research workbench
The structure basis of specific recognitions for substrates and inhibitors of rat monoamine oxidase a
Analyse The structure basis of specific recognitions for substrates and inhibitors of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O5W
- Type
- protein
- Length
- 2,032 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amine oxidase [flavin-containing] a
- EC
- 1.4.3.4
- UniProt
- P21396
- Ligands
- FAD, MLG
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 4 distinct chains · 37% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amine oxidase [flavin-containing] a (EC 1.4.3.4) | protein | 511 | 38% helix, 18% strand | P21396 |
| B | Amine oxidase [flavin-containing] a (EC 1.4.3.4) | protein | 503 | 36% helix, 19% strand | P21396 |
| C | Amine oxidase [flavin-containing] a (EC 1.4.3.4) | protein | 512 | 38% helix, 19% strand | P21396 |
| D | Amine oxidase [flavin-containing] a (EC 1.4.3.4) | protein | 506 | 36% helix, 19% strand | P21396 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- MLG · N-[3-(2,4-dichlorophenoxy)propyl]-N-methyl-N-prop-2-ynylamine · ligand · 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, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 457 | 0.88 | 0.95 | 68 | FAD, MLG |
| 2 | 464 | 0.88 | 0.95 | 68 | FAD, MLG |
| 3 | 475 | 0.87 | 0.94 | 69 | FAD, MLG |
| 4 | 771 | 0.85 | 0.88 | 103 | FAD, MLG |
| 5 | 987 | 0.76 | 0.78 | 111 | empty |
Interfaces
5 interfaces between chains.
- A–B · 2251 Ų buried · 32 hydrogen bonds · protein-protein
- C–D · 2234 Ų buried · 32 hydrogen bonds · protein-protein
- B–D · 599 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 189 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 184 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 cofactor (flavinylation).
Compared structures
- 1O5W · The structure basis of specific recognitions for substrates and inhibitors of rat… · the same entry in another collection · chain D against D, TM-score 1.00
- P21396 · AlphaFold monomer V2.0 prediction for amine oxidase [flavin- containing] a (P21396) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P21396
- Elsewhere: RCSB PDB 1O5W · PDBe 1O5W · UniProt P21396
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.