MolNFT v1 · #135066 · protein
Crystal structure of the E153Q mutant of the cftr inhibitory factor cif containing the adducted (R)-styrene oxide hydrolysis intermediate
5TNQ: “Crystal structure of the E153Q mutant of the cftr inhibitory factor cif containing the adducted (R)-styrene…”. X-ray diffraction, 1 ligand (FEH), 9 pockets (best druggability 0.81). MolNFT v1 #135066 on GenesisL1: 3D structure…
- PDB
- 5TNQ
- Type
- protein
- Length
- 1,172 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cftr inhibitory factor
- UniProt
- A0A0M3KL26
- Ligands
- FEH
- Pockets
- 9 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, D, A, B | Cftr inhibitory factor | protein | 293 | 44% helix, 18% strand | A0A0M3KL26 |
Ligands and binding sites
- FEH · (1R)-1-phenylethane-1,2-diol · ligand · 4 copies · chains C, D, A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 316 | 0.81 | 0.91 | 46 | empty |
| 2 | 382 | 0.79 | 0.89 | 57 | empty |
| 3 | 265 | 0.62 | 0.80 | 26 | empty |
| 4 | 241 | 0.61 | 0.81 | 28 | empty |
| 5 | 190 | 0.60 | 0.82 | 26 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1420 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1418 Ų buried · 12 hydrogen bonds · protein-protein
- C–B · 628 Ų buried · 4 hydrogen bonds · protein-protein
- D–A · 627 Ų buried · 4 hydrogen bonds · protein-protein
- C–A · 478 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent, 4 disulfide (covalent ligand, disulfide).
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 5TNQ · PDBe 5TNQ · UniProt A0A0M3KL26
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