Research workbench
R12E vflip mutant
Analyse R12E vflip mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PDJ
- Type
- protein
- Length
- 970 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flice inhibitory protein
- UniProt
- Q76RF1
- Pockets
- 12 · best druggability 0.80
Structure
x-ray diffraction · 6 distinct chains · 62% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flice inhibitory protein | protein | 166 | 63% helix, 0% strand | Q76RF1 |
| B | Flice inhibitory protein | protein | 157 | 61% helix, 0% strand | Q76RF1 |
| C | Flice inhibitory protein | protein | 164 | 62% helix, 0% strand | Q76RF1 |
| D | Flice inhibitory protein | protein | 165 | 61% helix, 0% strand | Q76RF1 |
| E | Flice inhibitory protein | protein | 159 | 63% helix, 0% strand | Q76RF1 |
| F | Flice inhibitory protein | protein | 159 | 61% helix, 0% strand | Q76RF1 |
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1138 | 0.80 | 0.82 | 112 | empty |
| 2 | 818 | 0.75 | 0.79 | 91 | empty |
| 3 | 152 | 0.72 | 0.90 | 30 | empty |
| 4 | 399 | 0.62 | 0.77 | 52 | empty |
| 5 | 354 | 0.62 | 0.78 | 38 | empty |
Interfaces
11 interfaces between chains.
- A–E · 346 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 306 Ų buried · 1 hydrogen bond · protein-protein
- B–E · 289 Ų buried · 0 hydrogen bonds · protein-protein
- A–F · 282 Ų buried · 0 hydrogen bonds · protein-protein
- D–E · 271 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 7PDJ · R12E vFLIP mutant · the same entry in another collection · chain A against A, TM-score 1.00
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 Q76RF1
- Elsewhere: RCSB PDB 7PDJ · PDBe 7PDJ · UniProt Q76RF1
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