MolNFT v1 · #1119 · protein
X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from escherichia COLI in open and closed form
1ARS: “X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from escherichia COLI…”. X-ray diffraction, 1 ligand (PLP), 5 pockets (best druggability 0.58). MolNFT v1 #1119 on GenesisL1: 3D structure…
- PDB
- 1ARS
- 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
- Pockets
- 5 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase (EC 2.6.1.1) | protein | 396 | 46% helix, 14% strand | P00509 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 256 | 0.58 | 0.78 | 45 | PLP |
| 2 | 63 | 0.38 | 0.80 | 22 | empty |
| 3 | 66 | 0.37 | 0.78 | 15 | empty |
| 4 | 69 | 0.29 | 0.73 | 17 | empty |
| 5 | 57 | 0.28 | 0.74 | 15 | empty |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 1ARS · X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases… · 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 1ARS · PDBe 1ARS · UniProt P00509
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