Research workbench
Crystal structures of escherichia COLI aspartate aminotransferase in two conformations: comparison of an unliganded open and two liganded closed forms
Analyse Crystal structures of escherichia COLI aspartate aminotransferase in two… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ASL
- 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
- PLA
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspartate aminotransferase (EC 2.6.1.1) | protein | 396 | 43% helix, 15% strand | P00509 |
Ligands and binding sites
- PLA · 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-2-methyl-succinic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 923 | 0.78 | 0.80 | 143 | PLA |
| 2 | 118 | 0.77 | 0.96 | 29 | PLA |
| 3 | 89 | 0.44 | 0.80 | 22 | empty |
| 4 | 69 | 0.40 | 0.79 | 14 | empty |
| 5 | 84 | 0.38 | 0.77 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 3411 Ų buried · 70 hydrogen bonds · protein-protein
Compared structures
- 1ASL · 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 B against A, TM-score 1.00
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 1ASL · PDBe 1ASL · UniProt P00509
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