Research workbench
Hydrocinnamic acid-bound structure of srhept + A293D mutant of E. COLI aspartate aminotransferase
Analyse Hydrocinnamic acid-bound structure of srhept + A293D mutant of E. COLI… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TOG
- 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
- HCI
- Pockets
- 13 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspartate aminotransferase (EC 2.6.1.1) | protein | 396 | 49% helix, 14% strand | P00509 |
Ligands and binding sites
- HCI · Hydrocinnamic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 527 | 0.71 | 0.80 | 69 | HCI |
| 2 | 58 | 0.70 | 0.98 | 17 | HCI |
| 3 | 202 | 0.52 | 0.77 | 35 | empty |
| 4 | 62 | 0.48 | 0.84 | 19 | empty |
| 5 | 104 | 0.39 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 3393 Ų buried · 59 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
Compared structures
- 1TOG · Hydrocinnamic acid-bound structure of SRHEPT + A293D mutant of E. coli aspartate… · 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 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 1TOG · PDBe 1TOG · UniProt P00509
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