MolNFT v1 · #134454 · protein
Plp and GABA trigger gabr-mediated transcription regulation in bacillus subsidies via external aldimine formation
5T4L · Aspartate aminotransferase: “Plp and GABA trigger gabr-mediated transcription regulation in bacillus subsidies via external aldimine…”. X-ray diffraction, 1 ligand (77E), 5 pockets (best druggability 0.60). MolNFT v1 #134454 on…
- PDB
- 5T4L
- 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
- 77E
- Pockets
- 5 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase (EC 2.6.1.1) | protein | 396 | 48% helix, 14% strand | P00509 |
Ligands and binding sites
- 77E · (4R)-4-amino-6-{3-hydroxy-2-methyl-5-[(phosphonooxy) methyl]pyridin-4-yl}hexanoic acid · 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 | 281 | 0.60 | 0.79 | 50 | 77E |
| 2 | 59 | 0.39 | 0.81 | 15 | empty |
| 3 | 78 | 0.39 | 0.77 | 19 | empty |
| 4 | 55 | 0.33 | 0.78 | 17 | empty |
| 5 | 85 | 0.33 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 5T4L · PLP and GABA Trigger GabR-Mediated Transcription Regulation in Bacillus subsidies via… · 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 5T4L · PDBe 5T4L · UniProt P00509
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