Research workbench
Thermus thermophilus aspartate aminotransferase tetra mutant 2
Analyse Thermus thermophilus aspartate aminotransferase tetra mutant 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5BJ4
- Type
- protein
- Length
- 732 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (aspartate aminotransferase)
- EC
- 2.6.1.1
- UniProt
- Q56232
- Ligands
- PLP, PO4
- Pockets
- 5 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (aspartate aminotransferase) (EC 2.6.1.1) | protein | 366 | 44% helix, 16% strand | Q56232 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 349 | 0.64 | 0.80 | 45 | PO4, PLP |
| 2 | 318 | 0.62 | 0.79 | 37 | PO4, PLP |
| 3 | 130 | 0.49 | 0.79 | 23 | empty |
| 4 | 123 | 0.48 | 0.79 | 25 | empty |
| 5 | 76 | 0.33 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 3084 Ų buried · 69 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 5BJ4 · Thermus thermophilus aspartate aminotransferase tetra mutant 2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q56232 · AlphaFold monomer V2.0 prediction for ASPARTATE/PREPHENATE aminotransferase (Q56232) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q56232
- Elsewhere: RCSB PDB 5BJ4 · PDBe 5BJ4 · UniProt Q56232
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