Research workbench
Structure of cytoplasmic aspartate aminotransferase from giardia lamblia
Analyse Structure of cytoplasmic aspartate aminotransferase from giardia lamblia in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MEB
- Type
- protein
- Length
- 852 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate aminotransferase
- EC
- 2.6.1.1
- UniProt
- A8B1V5
- Ligands
- PLP, SO4
- Pockets
- 11 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspartate aminotransferase (EC 2.6.1.1) | protein | 426 | 47% helix, 12% strand | A8B1V5 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 14 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.77 | 0.97 | 29 | EDO, SO4, PLP |
| 2 | 115 | 0.77 | 0.96 | 29 | SO4, PLP, EDO |
| 3 | 443 | 0.62 | 0.76 | 72 | EDO |
| 4 | 467 | 0.62 | 0.76 | 78 | EDO |
| 5 | 392 | 0.59 | 0.75 | 39 | empty |
Interfaces
1 interface between chains.
- A–B · 3402 Ų buried · 49 hydrogen bonds · protein-protein
Compared structures
- 3MEB · Structure of cytoplasmic aspartate aminotransferase from giardia lamblia · 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 A8B1V5
- Elsewhere: RCSB PDB 3MEB · PDBe 3MEB · UniProt A8B1V5
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