MolNFT v1 · #135057 · protein
Crystal structure of the E153Q mutant of the cftr inhibitory factor cif containing the adducted 17,18-epete hydrolysis intermediate
5TNH: “Crystal structure of the E153Q mutant of the cftr inhibitory factor cif containing the adducted 17,18-epete…”. X-ray diffraction, 1 ligand (7MS), 9 pockets (best druggability 0.78). MolNFT v1 #135057 on GenesisL1: 3D structure…
- PDB
- 5TNH
- Type
- protein
- Length
- 1,174 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cftr inhibitory factor
- UniProt
- A0A0M3KL26
- Ligands
- 7MS
- Pockets
- 9 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, D | Cftr inhibitory factor | protein | 293 | 44% helix, 19% strand | A0A0M3KL26 |
| A, B | Cftr inhibitory factor | protein | 294 | 43% helix, 20% strand | A0A0M3KL26 |
Ligands and binding sites
- 7MS · (5Z,8Z,11Z,14Z,17R,18R)-17,18-dihydroxyicosa-5,8,11,14-tetraenoic acid · 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, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 308 | 0.78 | 0.89 | 53 | empty |
| 2 | 298 | 0.77 | 0.89 | 48 | empty |
| 3 | 301 | 0.65 | 0.81 | 39 | 7MS |
| 4 | 246 | 0.62 | 0.81 | 34 | empty |
| 5 | 287 | 0.62 | 0.80 | 34 | 7MS |
Interfaces
5 interfaces between chains.
- A–B · 1467 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 1440 Ų buried · 15 hydrogen bonds · protein-protein
- D–A · 679 Ų buried · 6 hydrogen bonds · protein-protein
- C–B · 660 Ų buried · 8 hydrogen bonds · protein-protein
- C–A · 496 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent, 4 disulfide (covalent ligand, disulfide).
Compared structures
- 5TNH · Crystal structure of the E153Q mutant of the CFTR inhibitory factor Cif containing the… · the same entry in another collection · chain D against D, 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 5TNH · PDBe 5TNH · UniProt A0A0M3KL26
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.