Research workbench
Structure of a mitochondrial aspartate aminotransferase from trypanosoma brucei
Analyse Structure of a mitochondrial aspartate aminotransferase from trypanosoma brucei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EU1
- Type
- protein
- Length
- 764 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitochondrial aspartate aminotransferase
- EC
- 2.6.1.1
- UniProt
- Q964F0
- Ligands
- CL
- Pockets
- 8 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitochondrial aspartate aminotransferase (EC 2.6.1.1) | protein | 383 | 48% helix, 14% strand | Q964F0 |
| B | Mitochondrial aspartate aminotransferase (EC 2.6.1.1) | protein | 381 | 48% helix, 14% strand | Q964F0 |
Ligands and binding sites
- CL · Chloride ion · ion · 5 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 3 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 523 | 0.65 | 0.77 | 44 | empty |
| 2 | 397 | 0.58 | 0.75 | 31 | empty |
| 3 | 59 | 0.42 | 0.82 | 23 | empty |
| 4 | 62 | 0.38 | 0.78 | 13 | empty |
| 5 | 83 | 0.35 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1737 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
Compared structures
- 4EU1 · Structure of a mitochondrial aspartate aminotransferase from Trypanosoma brucei · 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 Q964F0
- Elsewhere: RCSB PDB 4EU1 · PDBe 4EU1 · UniProt Q964F0
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