Research workbench
Mao inhibition by rasagiline analogues
Analyse Mao inhibition by rasagiline analogues in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C65
- Type
- protein
- Length
- 993 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amine oxidase [flavin-containing] B
- EC
- 1.4.3.4
- UniProt
- P27338
- Ligands
- FAD, 4CR
- Pockets
- 13 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amine oxidase [flavin-containing] B (EC 1.4.3.4) | protein | 499 | 39% helix, 20% strand | P27338 |
| B | Amine oxidase [flavin-containing] B (EC 1.4.3.4) | protein | 494 | 39% helix, 20% strand | P27338 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- 4CR · (1R)-4-({[ethyl(methyl)amino]carbonyl}oxy)-N-methyl-N-[(1E)-prop-2-en-1-ylidene]indan-1-aminium · ligand · 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, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 417 | 0.88 | 0.96 | 66 | FAD, 4CR |
| 2 | 421 | 0.87 | 0.95 | 68 | FAD, 4CR |
| 3 | 282 | 0.58 | 0.78 | 40 | empty |
| 4 | 226 | 0.56 | 0.78 | 28 | empty |
| 5 | 237 | 0.54 | 0.77 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 2124 Ų buried · 38 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (flavinylation).
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 P27338
- Elsewhere: RCSB PDB 2C65 · PDBe 2C65 · UniProt P27338
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