Research workbench
Structure of a mitochondrial aspartate aminotransferase from trypanosoma brucei, K237A mutant
Analyse Structure of a mitochondrial aspartate aminotransferase from trypanosoma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4W5K
- Type
- protein
- Length
- 760 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate aminotransferase, mitochondrial
- EC
- 2.6.1.1
- UniProt
- Q385Q9
- Ligands
- PLP, MLT
- Pockets
- 7 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspartate aminotransferase, mitochondrial (EC 2.6.1.1) | protein | 380 | 47% helix, 14% strand | Q385Q9 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- MLT · D-malate · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 402 | 0.66 | 0.79 | 45 | PLP |
| 2 | 339 | 0.65 | 0.80 | 40 | PLP |
| 3 | 64 | 0.42 | 0.81 | 23 | empty |
| 4 | 70 | 0.40 | 0.79 | 13 | empty |
| 5 | 84 | 0.36 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1689 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 4W5K · Structure of a mitochondrial aspartate aminotransferase from Trypanosoma brucei, K237A… · 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 Q385Q9
- Elsewhere: RCSB PDB 4W5K · PDBe 4W5K · UniProt Q385Q9
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