Research workbench
Mechanism of inactivation of E. COLI aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-furancarboxylic acid (S-adfa) pH 7.5
Analyse Mechanism of inactivation of E. COLI aspartate aminotransferase by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PA9
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate aminotransferase
- EC
- 2.6.1.1
- UniProt
- D3H0F7
- Ligands
- PJ7, PMP, SO4
- Pockets
- 7 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase (EC 2.6.1.1) | protein | 396 | 47% helix, 14% strand | D3H0F7 |
Ligands and binding sites
- PJ7 · 4-aminofuran-2-carboxylic acid · ligand · chains A
- PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
- GOL · Glycerol · additive · 11 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 296 | 0.60 | 0.79 | 48 | PJ7, PMP |
| 2 | 100 | 0.41 | 0.77 | 23 | GOL |
| 3 | 83 | 0.40 | 0.78 | 18 | empty |
| 4 | 62 | 0.37 | 0.78 | 17 | empty |
| 5 | 95 | 0.35 | 0.75 | 18 | GOL |
Modifications
Observed in the structure: 2 covalent (additive adduct, covalent ligand).
Compared structures
- 3PA9 · Mechanism of inactivation of E. coli aspartate aminotransferase by… · 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 D3H0F7
- Elsewhere: RCSB PDB 3PA9 · PDBe 3PA9 · UniProt D3H0F7
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