Research workbench
Crystal structure of the cftr inhibitory factor cif with the H177Y mutation
Analyse Crystal structure of the cftr inhibitory factor cif with the H177Y mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PI6
- Type
- protein
- Length
- 1,187 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydrolase
- UniProt
- Q02P97
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydrolase | protein | 297 | 42% helix, 20% strand | Q02P97 |
| B, C | Hydrolase | protein | 296 | 42% helix, 20% strand | Q02P97 |
| D | Hydrolase | protein | 298 | 43% helix, 19% strand | Q02P97 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 281 | 0.79 | 0.91 | 40 | empty |
| 2 | 305 | 0.77 | 0.89 | 48 | empty |
| 3 | 353 | 0.64 | 0.79 | 50 | empty |
| 4 | 247 | 0.61 | 0.80 | 29 | empty |
| 5 | 244 | 0.60 | 0.80 | 29 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1421 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1410 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 639 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 630 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 391 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3PI6 · Crystal structure of the CFTR inhibitory factor Cif with the H177Y mutation · 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 Q02P97
- Elsewhere: RCSB PDB 3PI6 · PDBe 3PI6 · UniProt Q02P97
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