Research workbench
Crystal structure of the cftr inhibitory factor cif with the E153Q mutation adducted with the 1,2-epoxyhexane hydrolysis intermediate
Analyse Crystal structure of the cftr inhibitory factor cif with the E153Q mutation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DNO
- Type
- protein
- Length
- 1,181 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative hydrolase
- UniProt
- Q02P97
- Ligands
- 7FB
- Pockets
- 9 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Putative hydrolase | protein | 297 | 42% helix, 18% strand | Q02P97 |
| B | Putative hydrolase | protein | 293 | 43% helix, 20% strand | Q02P97 |
| D | Putative hydrolase | protein | 294 | 43% helix, 20% strand | Q02P97 |
Ligands and binding sites
- 7FB · (2R)-hexane-1,2-diol · ligand · 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, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 275 | 0.82 | 0.93 | 42 | empty |
| 2 | 342 | 0.79 | 0.89 | 49 | empty |
| 3 | 273 | 0.62 | 0.80 | 34 | empty |
| 4 | 237 | 0.59 | 0.80 | 30 | empty |
| 5 | 173 | 0.56 | 0.81 | 18 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1426 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 1416 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 629 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 621 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 469 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent, 4 disulfide (covalent ligand, disulfide).
Compared structures
- 4DNO · Crystal structure of the CFTR inhibitory factor Cif with the E153Q mutation adducted with… · 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 4DNO · PDBe 4DNO · UniProt Q02P97
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