Research workbench
L-tryptophan aminotransferase
Analyse L-tryptophan aminotransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BWN
- Type
- protein
- Length
- 2,173 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-tryptophan aminotransferase
- UniProt
- Q9S7N2
- Ligands
- PMP, PHE, PO4
- Pockets
- 17 · best druggability 0.73
Structure
x-ray diffraction · 6 distinct chains · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-tryptophan aminotransferase | protein | 362 | 36% helix, 19% strand | Q9S7N2 |
| B | L-tryptophan aminotransferase | protein | 369 | 35% helix, 18% strand | Q9S7N2 |
| C | L-tryptophan aminotransferase | protein | 361 | 38% helix, 18% strand | Q9S7N2 |
| D | L-tryptophan aminotransferase | protein | 359 | 36% helix, 19% strand | Q9S7N2 |
| E | L-tryptophan aminotransferase | protein | 362 | 36% helix, 16% strand | Q9S7N2 |
| F | L-tryptophan aminotransferase | protein | 360 | 38% helix, 19% strand | Q9S7N2 |
Ligands and binding sites
- PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · 4 copies · chains A, B, C, D, E, F
- PHE · Phenylalanine · ligand · chains E, F
- PO4 · Phosphate ion · ion · chains E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 317 | 0.73 | 0.85 | 34 | PO4 |
| 2 | 301 | 0.72 | 0.85 | 34 | PMP |
| 3 | 340 | 0.72 | 0.84 | 39 | PMP |
| 4 | 293 | 0.72 | 0.85 | 34 | PMP |
| 5 | 364 | 0.71 | 0.83 | 44 | PMP, PHE |
Interfaces
5 interfaces between chains.
- C–D · 2523 Ų buried · 64 hydrogen bonds · protein-protein
- A–B · 2480 Ų buried · 60 hydrogen bonds · protein-protein
- E–F · 2451 Ų buried · 54 hydrogen bonds · protein-protein
- A–F · 284 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 67 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (cofactor).
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 Q9S7N2
- Elsewhere: RCSB PDB 3BWN · PDBe 3BWN · UniProt Q9S7N2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.