MolNFT v1 · #81690 · protein
Crystal structures of branched-chain aminotransferase from deinococcus radiodurans complexes with alpha-ketoisocaproate and L-glutamate suggest its radio-resistance for catalysis
3UZO · Branched-chain-amino-acid aminotransferase: “Crystal structures of branched-chain aminotransferase from deinococcus radiodurans complexes with…”. X-ray diffraction, 2 ligands (PLP, GLU), 8 pockets (best druggability 0.79). MolNFT v1…
- PDB
- 3UZO
- Type
- protein
- Length
- 670 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, GLU
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Branched-chain-amino-acid aminotransferase (EC 2.6.1.42) | protein | 335 | 25% helix, 30% strand | Q9RTX5 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- GLU · Glutamic acid · 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, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.79 | 0.97 | 32 | PLP, GLU |
| 2 | 415 | 0.77 | 0.86 | 55 | PLP, GLU |
| 3 | 51 | 0.71 | 0.99 | 20 | empty |
| 4 | 130 | 0.55 | 0.82 | 31 | empty |
| 5 | 151 | 0.50 | 0.79 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 2576 Ų buried · 42 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 3UZO · 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 3UZO · PDBe 3UZO · UniProt Q9RTX5
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