Research workbench
Crystal structure of a putative aspartate aminotransferase from leishmania major friedlin
Analyse Crystal structure of a putative aspartate aminotransferase from leishmania… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4H51
- Type
- protein
- Length
- 801 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate aminotransferase
- EC
- 2.6.1.1
- UniProt
- Q4FX34
- Pockets
- 8 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase (EC 2.6.1.1) | protein | 398 | 49% helix, 14% strand | Q4FX34 |
| B | Aspartate aminotransferase (EC 2.6.1.1) | protein | 403 | 49% helix, 14% strand | Q4FX34 |
Ligands and binding sites
- 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
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 | 72 | 0.73 | 0.97 | 21 | empty |
| 2 | 51 | 0.67 | 0.96 | 16 | empty |
| 3 | 53 | 0.67 | 0.96 | 15 | empty |
| 4 | 496 | 0.61 | 0.75 | 66 | empty |
| 5 | 337 | 0.57 | 0.75 | 42 | empty |
Interfaces
1 interface between chains.
- A–B · 3824 Ų buried · 54 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
Compared structures
- 4H51 · Crystal structure of a putative Aspartate Aminotransferase from Leishmania major Friedlin · 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 Q4FX34
- Elsewhere: RCSB PDB 4H51 · PDBe 4H51 · UniProt Q4FX34
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