Research workbench
Arabidopsis thaliana prephenate aminotransferase mutant- T84V
Analyse Arabidopsis thaliana prephenate aminotransferase mutant- T84V in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WMI
- Type
- protein
- Length
- 402 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional aspartate aminotransferase and GLUTAMATE/ASPARTATE-prephenate…
- EC
- 2.6.1.1, 2.6.1.78, 2.6.1.79
- UniProt
- Q9SIE1
- Ligands
- AKG
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional aspartate aminotransferase and GLUTAMATE/ASPARTATE-prephenate aminotransferase (EC 2.6.1.1, 2.6.1.78, 2.6.1.79) | protein | 402 | 45% helix, 15% strand | Q9SIE1 |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · 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 | 183 | 0.67 | 0.86 | 32 | AKG |
| 2 | 55 | 0.29 | 0.75 | 13 | empty |
| 3 | 67 | 0.29 | 0.73 | 16 | empty |
| 4 | 56 | 0.28 | 0.74 | 12 | empty |
Compared structures
- 5WMI · Arabidopsis thaliana Prephenate Aminotransferase mutant- T84V · the same entry in another collection · chain A against A, TM-score 1.00
- Q9SIE1 · AlphaFold monomer V2.0 prediction for bifunctional aspartate aminotransferase and… · a predicted model of the same protein · chain A 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 Q9SIE1
- Elsewhere: RCSB PDB 5WMI · PDBe 5WMI · UniProt Q9SIE1
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