Research workbench
The structural basis for the reduced activity of the D223A(D222A) active site mutant of E. COLI aspartate aminotransferase
Analyse The structural basis for the reduced activity of the D223A(D222A) active site… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ASC
- 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
- P00509
- Ligands
- NPL
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase (EC 2.6.1.1) | protein | 396 | 44% helix, 15% strand | P00509 |
Ligands and binding sites
- NPL · N-methyl-4-deoxy-4-amino-pyridoxal-5-phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 263 | 0.64 | 0.81 | 45 | NPL |
| 2 | 107 | 0.41 | 0.77 | 21 | empty |
| 3 | 62 | 0.32 | 0.76 | 15 | empty |
| 4 | 53 | 0.28 | 0.74 | 17 | empty |
Compared structures
- 1ASC · The structural basis for the reduced activity of the D223A(D222A) active site mutant of… · the same entry in another collection · chain A against A, TM-score 1.00
- P00509 · AlphaFold monomer V2.0 prediction for aspartate aminotransferase (P00509) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00509
- Elsewhere: RCSB PDB 1ASC · PDBe 1ASC · UniProt P00509
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