Research workbench
Crystal structure of the cftr inhibitory factor cif with the H269A mutation
Analyse Crystal structure of the cftr inhibitory factor cif with the H269A mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KDA
- Type
- protein
- Length
- 1,192 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cftr inhibitory factor (cif)
- UniProt
- Q02P97
- Pockets
- 10 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, C, A, B | Cftr inhibitory factor (cif) | protein | 298 | 43% helix, 20% strand | Q02P97 |
Pockets
10 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 297 | 0.77 | 0.89 | 47 | empty |
| 2 | 193 | 0.77 | 0.92 | 38 | empty |
| 3 | 50 | 0.71 | 0.99 | 19 | empty |
| 4 | 601 | 0.71 | 0.79 | 63 | empty |
| 5 | 56 | 0.71 | 0.97 | 19 | empty |
Interfaces
5 interfaces between chains.
- D–C · 1416 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1402 Ų buried · 14 hydrogen bonds · protein-protein
- C–B · 591 Ų buried · 5 hydrogen bonds · protein-protein
- D–A · 587 Ų buried · 5 hydrogen bonds · protein-protein
- C–A · 377 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3KDA · Crystal structure of the CFTR inhibitory factor Cif with the H269A mutation · the same entry in another collection · chain D against D, 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 3KDA · PDBe 3KDA · UniProt Q02P97
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