MolNFT v1 · #1136 · protein
The structural basis for the reduced activity of the D223A(D222A) active site mutant of E. COLI aspartate aminotransferase
1ASB: “The structural basis for the reduced activity of the D223A(D222A) active site mutant of E. COLI aspartate…”. X-ray diffraction, 2 ligands (PLP, MAE), 8 pockets (best druggability 0.70). MolNFT v1 #1136 on GenesisL1: 3D structure…
- PDB
- 1ASB
- 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
- PLP, MAE
- Pockets
- 8 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase (EC 2.6.1.1) | protein | 396 | 45% helix, 13% strand | P00509 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 255 | 0.70 | 0.85 | 32 | PLP, MAE |
| 2 | 111 | 0.42 | 0.76 | 24 | empty |
| 3 | 50 | 0.35 | 0.79 | 13 | empty |
| 4 | 67 | 0.34 | 0.76 | 23 | empty |
| 5 | 65 | 0.33 | 0.76 | 21 | empty |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 1ASB · 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 1ASB · PDBe 1ASB · UniProt P00509
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