Research workbench
Tyrosine aminotransferase from E. COLI
Analyse Tyrosine aminotransferase from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TAT
- Type
- protein
- Length
- 2,382 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine aminotransferase
- EC
- 2.6.1.57
- UniProt
- P04693
- Ligands
- PLP
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Tyrosine aminotransferase (EC 2.6.1.57) | protein | 397 | 41% helix, 7% strand | P04693 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 269 | 0.75 | 0.88 | 47 | empty |
| 2 | 190 | 0.74 | 0.89 | 32 | empty |
| 3 | 174 | 0.74 | 0.90 | 30 | empty |
| 4 | 273 | 0.73 | 0.87 | 43 | empty |
| 5 | 179 | 0.73 | 0.90 | 30 | empty |
Interfaces
4 interfaces between chains.
- A–B · 3066 Ų buried · 43 hydrogen bonds · protein-protein
- E–F · 2971 Ų buried · 40 hydrogen bonds · protein-protein
- C–D · 2941 Ų buried · 39 hydrogen bonds · protein-protein
- A–E · 439 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 cofactor (pyridoxal phosphate Schiff base).
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 P04693
- Elsewhere: RCSB PDB 3TAT · PDBe 3TAT · UniProt P04693
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