Research workbench
Crystal structure of the cftr inhibitory factor cif bound to 1,2- hexanediol
Analyse Crystal structure of the cftr inhibitory factor cif bound to 1,2- hexanediol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EUS
- Type
- protein
- Length
- 1,172 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative hydrolase
- UniProt
- Q02P97
- Ligands
- 0RE
- Pockets
- 9 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Putative hydrolase | protein | 293 | 43% helix, 20% strand | Q02P97 |
Ligands and binding sites
- 0RE · (2S)-hexane-1,2-diol · ligand · 2 copies · chains B, 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 | 296 | 0.78 | 0.90 | 46 | empty |
| 2 | 487 | 0.76 | 0.84 | 72 | empty |
| 3 | 53 | 0.69 | 0.97 | 19 | 0RE |
| 4 | 55 | 0.69 | 0.97 | 19 | 0RE |
| 5 | 241 | 0.63 | 0.81 | 30 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1417 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1408 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 643 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 641 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 397 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4EUS · Crystal structure of the CFTR inhibitory factor Cif bound to 1,2-hexanediol · 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 4EUS · PDBe 4EUS · UniProt Q02P97
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