MolNFT v1 · #135054 · protein
Crystal structure of the E153Q mutant of the cftr inhibitory factor cif containing the adducted cis-stilbene oxide hydrolysis intermediate
5TNE: “Crystal structure of the E153Q mutant of the cftr inhibitory factor cif containing the adducted cis-stilbene…”. X-ray diffraction, 1 ligand (7F6), 10 pockets (best druggability 0.80). MolNFT v1 #135054 on GenesisL1: 3D structure…
- PDB
- 5TNE
- Type
- protein
- Length
- 1,186 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cftr inhibitory factor
- UniProt
- A0A0M3KL26
- Ligands
- 7F6
- Pockets
- 10 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Cftr inhibitory factor | protein | 297 | 43% helix, 18% strand | A0A0M3KL26 |
| B, D | Cftr inhibitory factor | protein | 296 | 44% helix, 20% strand | A0A0M3KL26 |
Ligands and binding sites
- 7F6 · (1R,2R)-1,2-diphenylethane-1,2-diol · ligand · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 306 | 0.80 | 0.91 | 45 | empty |
| 2 | 338 | 0.79 | 0.89 | 51 | empty |
| 3 | 52 | 0.72 | 0.99 | 18 | 7F6 |
| 4 | 53 | 0.70 | 0.98 | 18 | empty |
| 5 | 50 | 0.70 | 0.98 | 17 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1430 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1423 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 631 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 624 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 486 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 5TNE · PDBe 5TNE · UniProt A0A0M3KL26
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