Research workbench
Crystal structure of the cftr inhibitory factor cif with the Y239F mutation
Analyse Crystal structure of the cftr inhibitory factor cif with the Y239F mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DMK
- Type
- protein
- Length
- 1,186 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative hydrolase
- UniProt
- Q02P97
- Pockets
- 10 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Putative hydrolase | protein | 296 | 43% helix, 20% strand | Q02P97 |
| B, C | Putative hydrolase | protein | 297 | 43% helix, 20% strand | Q02P97 |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 264 | 0.79 | 0.91 | 40 | empty |
| 2 | 276 | 0.78 | 0.90 | 43 | empty |
| 3 | 56 | 0.72 | 0.98 | 19 | GOL |
| 4 | 64 | 0.72 | 0.97 | 19 | GOL |
| 5 | 52 | 0.71 | 0.98 | 19 | GOL |
Interfaces
5 interfaces between chains.
- A–B · 1421 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1406 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 639 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 625 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 387 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4DMK · Crystal structure of the CFTR inhibitory factor Cif with the Y239F 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 4DMK · PDBe 4DMK · UniProt Q02P97
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