Research workbench
Crystal structure of aat D222T mutant
Analyse Crystal structure of aat D222T mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TOR
- Type
- protein
- Length
- 826 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate aminotransferase, cytoplasmic
- EC
- 2.6.1.1, 2.6.1.3
- UniProt
- P00503
- Pockets
- 11 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase, cytoplasmic (EC 2.6.1.1, 2.6.1.3) | protein | 414 | 46% helix, 13% strand | P00503 |
| B | Aspartate aminotransferase, cytoplasmic (EC 2.6.1.1, 2.6.1.3) | protein | 412 | 45% helix, 13% strand | P00503 |
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 747 | 0.72 | 0.78 | 72 | empty |
| 2 | 147 | 0.72 | 0.91 | 29 | empty |
| 3 | 543 | 0.71 | 0.80 | 45 | empty |
| 4 | 108 | 0.59 | 0.85 | 18 | empty |
| 5 | 111 | 0.49 | 0.80 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 3431 Ų buried · 56 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
Compared structures
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 P00503
- Elsewhere: RCSB PDB 5TOR · PDBe 5TOR · UniProt P00503
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.