Research workbench
Crystal structure of mouse tifa (T9D/C36S mutant)
Analyse Crystal structure of mouse tifa (T9D/C36S mutant) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L9V
- Type
- protein
- Length
- 555 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Traf-interacting protein with fha domain-containing protein a
- UniProt
- Q793I8
- Pockets
- 5 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | Traf-interacting protein with fha domain-containing protein a | protein | 139 | 2% helix, 48% strand | Q793I8 |
| B | Traf-interacting protein with fha domain-containing protein a | protein | 138 | 2% helix, 47% strand | Q793I8 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 914 | 0.87 | 0.89 | 86 | empty |
| 2 | 127 | 0.59 | 0.84 | 23 | empty |
| 3 | 103 | 0.57 | 0.85 | 25 | empty |
| 4 | 58 | 0.31 | 0.75 | 12 | empty |
| 5 | 61 | 0.29 | 0.74 | 11 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1103 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 1091 Ų buried · 19 hydrogen bonds · protein-protein
- B–D · 577 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 550 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 124 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6L9V · Crystal structure of mouse TIFA (T9D/C36S mutant) · the same entry in another collection · chain A against A, TM-score 1.00
- Q793I8 · AlphaFold monomer V2.0 prediction for traf-interacting protein with fha domain-containing… · a predicted model of the same protein · chain A 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 Q793I8
- Elsewhere: RCSB PDB 6L9V · PDBe 6L9V · UniProt Q793I8
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