Research workbench
Intercoversion of substrate specificity: E. COLI aspatate aminotransferase to tyrosine aminotransferase: chimera P3.
Analyse Intercoversion of substrate specificity: E. COLI aspatate aminotransferase to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F5H
- Type
- protein
- Length
- 797 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
- Pockets
- 15 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase (EC 2.6.1.1) | protein | 397 | 48% helix, 14% strand | P00509 |
| B | Aspartate aminotransferase (EC 2.6.1.1) | protein | 400 | 48% helix, 14% strand | P00509 |
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 672 | 0.71 | 0.78 | 49 | empty |
| 2 | 663 | 0.70 | 0.77 | 44 | empty |
| 3 | 118 | 0.54 | 0.83 | 28 | empty |
| 4 | 132 | 0.53 | 0.81 | 31 | empty |
| 5 | 128 | 0.43 | 0.77 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 3146 Ų buried · 58 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
Compared structures
- 4F5H · Intercoversion of Substrate Specificity: E. coli Aspatate Aminotransferase to Tyrosine… · 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 0.98
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 4F5H · PDBe 4F5H · UniProt P00509
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