Research workbench
Crystal structure of the cftr inhibitory factor cif bound to the inhibitor KB2115
Analyse Crystal structure of the cftr inhibitory factor cif bound to the inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HKB
- Type
- protein
- Length
- 1,188 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cftr inhibitory factor (cif)
- UniProt
- A0A0M3KL26
- Ligands
- 64L
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Cftr inhibitory factor (cif) | protein | 297 | 42% helix, 20% strand | A0A0M3KL26 |
Ligands and binding sites
- 64L · Kb2115 · ligand · 4 copies · chains A, B, C, D
- ACT · Acetate ion · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 586 | 0.79 | 0.85 | 78 | 64L, ACT |
| 2 | 377 | 0.77 | 0.87 | 56 | empty |
| 3 | 487 | 0.72 | 0.82 | 53 | 64L, ACT |
| 4 | 173 | 0.63 | 0.84 | 24 | 64L, ACT |
| 5 | 276 | 0.62 | 0.80 | 30 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1432 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1418 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 670 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 663 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 424 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5HKB · Crystal structure of the CFTR inhibitory factor Cif bound to the inhibitor KB2115 · 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 A0A0M3KL26
- Elsewhere: RCSB PDB 5HKB · PDBe 5HKB · UniProt A0A0M3KL26
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