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Crystal structure of aat H143L mutant
Analyse Crystal structure of aat H143L mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TON
- Type
- protein
- Length
- 810 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 0.71
Structure
x-ray diffraction · 2 distinct chains · 45% 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 | 45% helix, 13% strand | P00503 |
| B | Aspartate aminotransferase, cytoplasmic (EC 2.6.1.1, 2.6.1.3) | protein | 396 | 44% helix, 13% strand | P00503 |
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.71 | 0.91 | 28 | empty |
| 2 | 683 | 0.70 | 0.78 | 59 | empty |
| 3 | 146 | 0.59 | 0.83 | 28 | empty |
| 4 | 257 | 0.53 | 0.76 | 42 | empty |
| 5 | 124 | 0.50 | 0.80 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 3301 Ų buried · 55 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 5TON · PDBe 5TON · UniProt P00503
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