Research workbench
Crystal structures of branched-chain aminotransferase from deinococcus radiodurans complexes with alpha-ketoisocaproate and L-glutamate suggest its radio-resistance for catalysis
Analyse Crystal structures of branched-chain aminotransferase from deinococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UYY
- Type
- protein
- Length
- 672 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Branched-chain-amino-acid aminotransferase
- EC
- 2.6.1.42
- UniProt
- Q9RTX5
- Ligands
- PLP
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Branched-chain-amino-acid aminotransferase (EC 2.6.1.42) | protein | 335 | 24% helix, 29% strand | Q9RTX5 |
| B | Branched-chain-amino-acid aminotransferase (EC 2.6.1.42) | protein | 337 | 25% helix, 31% strand | Q9RTX5 |
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
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 124 | 0.78 | 0.96 | 27 | PLP |
| 2 | 475 | 0.75 | 0.84 | 57 | PLP |
| 3 | 50 | 0.70 | 0.98 | 22 | empty |
| 4 | 132 | 0.53 | 0.81 | 30 | empty |
| 5 | 54 | 0.48 | 0.85 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 2627 Ų buried · 42 hydrogen bonds · protein-protein
Compared structures
- 3UYY · Crystal Structures of Branched-Chain Aminotransferase from Deinococcus radiodurans… · 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 Q9RTX5
- Elsewhere: RCSB PDB 3UYY · PDBe 3UYY · UniProt Q9RTX5
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