MolNFT v1 · #135058 · protein
Crystal structure of the E153Q mutant of the cftr inhibitory factor cif containing the adducted S-styrene oxide hydrolysis intermediate
5TNI: “Crystal structure of the E153Q mutant of the cftr inhibitory factor cif containing the adducted S-styrene…”. X-ray diffraction, 1 ligand (FEH), 10 pockets (best druggability 0.79). MolNFT v1 #135058 on GenesisL1: 3D structure…
- PDB
- 5TNI
- Type
- protein
- Length
- 1,183 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cftr inhibitory factor
- UniProt
- A0A0M3KL26
- Ligands
- FEH
- Pockets
- 10 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Cftr inhibitory factor | protein | 297 | 42% helix, 18% strand | A0A0M3KL26 |
| B | Cftr inhibitory factor | protein | 293 | 43% helix, 20% strand | A0A0M3KL26 |
| C | Cftr inhibitory factor | protein | 296 | 42% helix, 18% strand | A0A0M3KL26 |
Ligands and binding sites
- FEH · (1R)-1-phenylethane-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
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 289 | 0.79 | 0.91 | 45 | empty |
| 2 | 613 | 0.77 | 0.83 | 84 | empty |
| 3 | 242 | 0.62 | 0.81 | 29 | empty |
| 4 | 272 | 0.62 | 0.80 | 30 | empty |
| 5 | 173 | 0.57 | 0.81 | 19 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1432 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 1412 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 639 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 599 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 451 Ų buried · 10 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 5TNI · PDBe 5TNI · UniProt A0A0M3KL26
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