Research workbench
Crystal structure of aspartate aminotransferase from trypanosoma cruzi at 2.07 ångström resolution
Analyse Crystal structure of aspartate aminotransferase from trypanosoma cruzi at 2.07… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EZL
- Type
- protein
- Length
- 784 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate aminotransferase
- EC
- 2.6.1.1
- UniProt
- Q4D080
- Ligands
- PLP
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase (EC 2.6.1.1) | protein | 392 | 47% helix, 14% strand | Q4D080 |
| B | Aspartate aminotransferase (EC 2.6.1.1) | protein | 392 | 48% helix, 14% strand | Q4D080 |
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
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1100 | 0.76 | 0.78 | 128 | empty |
| 2 | 57 | 0.72 | 0.98 | 22 | empty |
| 3 | 102 | 0.42 | 0.77 | 28 | empty |
| 4 | 90 | 0.40 | 0.78 | 16 | empty |
| 5 | 79 | 0.38 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 2674 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 6EZL · Crystal structure of aspartate aminotransferase from Trypanosoma cruzi at 2.07 Angstrom… · 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 Q4D080
- Elsewhere: RCSB PDB 6EZL · PDBe 6EZL · UniProt Q4D080
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