MolNFT v1 · #1146 · protein
Crystal structures of escherichia COLI aspartate aminotransferase in two conformations: comparison of an unliganded open and two liganded closed forms
1ASM: “Crystal structures of escherichia COLI aspartate aminotransferase in two conformations: comparison of an…”. X-ray diffraction, 2 ligands (PLP, MAE), 11 pockets (best druggability 0.78). MolNFT v1 #1146 on GenesisL1: 3D structure…
- PDB
- 1ASM
- Type
- protein
- Length
- 792 residues
- Chains
- 2
- 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
- 11 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspartate aminotransferase (EC 2.6.1.1) | protein | 396 | 47% helix, 14% strand | P00509 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- MAE · Maleic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.78 | 0.97 | 29 | PLP, MAE |
| 2 | 112 | 0.77 | 0.97 | 30 | PLP, MAE |
| 3 | 387 | 0.61 | 0.77 | 58 | empty |
| 4 | 167 | 0.49 | 0.77 | 27 | empty |
| 5 | 74 | 0.39 | 0.78 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 3449 Ų buried · 64 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 1ASM · Crystal structures of escherichia COLI aspartate aminotransferase in two conformations… · 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 1ASM · PDBe 1ASM · UniProt P00509
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