MolNFT v1 · #21913 · protein
Role of ASP222 in the catalytic mechanism of escherichia COLI aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate
1SPA: “Role of ASP222 in the catalytic mechanism of escherichia COLI aspartate aminotransferase: the amino acid…”. X-ray diffraction, 1 ligand (NPL), 4 pockets (best druggability 0.64). MolNFT v1 #21913 on GenesisL1: 3D structure, binding…
- PDB
- 1SPA
- 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 · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase (EC 2.6.1.1) | protein | 396 | 47% 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 | 255 | 0.64 | 0.82 | 41 | NPL |
| 2 | 78 | 0.40 | 0.78 | 21 | empty |
| 3 | 53 | 0.33 | 0.78 | 20 | empty |
| 4 | 55 | 0.24 | 0.72 | 17 | empty |
Compared structures
- 1SPA · Role of ASP222 in the catalytic mechanism of escherichia COLI aspartate aminotransferase… · 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 1SPA · PDBe 1SPA · UniProt P00509
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