Research workbench
Hypothetical alanine aminotransferase (TTH0173) from thermus thermophilus HB8
Analyse Hypothetical alanine aminotransferase (TTH0173) from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YRR
- Type
- protein
- Length
- 704 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminotransferase, class V
- EC
- 2.6.1.-
- UniProt
- Q5SLX0
- Ligands
- PLP
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aminotransferase, class V (EC 2.6.1.-) | protein | 352 | 45% helix, 16% strand | Q5SLX0 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 272 | 0.64 | 0.81 | 32 | empty |
| 2 | 236 | 0.63 | 0.81 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 1942 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 2YRR · hypothetical alanine aminotransferase (TTH0173) from Thermus thermophilus HB8 · the same entry in another collection · 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 Q5SLX0
- Elsewhere: RCSB PDB 2YRR · PDBe 2YRR · UniProt Q5SLX0
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