MolNFT v1 · #135056 · protein
Crystal structure of the E153Q mutant of the cftr inhibitory factor cif containing the adducted 14,15-epete hydrolysis intermediate
5TNG: “Crystal structure of the E153Q mutant of the cftr inhibitory factor cif containing the adducted 14,15-epete…”. X-ray diffraction, 1 ligand (7LE), 9 pockets (best druggability 0.80). MolNFT v1 #135056 on GenesisL1: 3D structure…
- PDB
- 5TNG
- Type
- protein
- Length
- 1,180 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cftr inhibitory factor
- UniProt
- A0A0M3KL26
- Ligands
- 7LE
- Pockets
- 9 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cftr inhibitory factor | protein | 296 | 43% helix, 18% strand | A0A0M3KL26 |
| B | Cftr inhibitory factor | protein | 294 | 44% helix, 20% strand | A0A0M3KL26 |
| C | Cftr inhibitory factor | protein | 293 | 43% helix, 18% strand | A0A0M3KL26 |
| D | Cftr inhibitory factor | protein | 297 | 42% helix, 20% strand | A0A0M3KL26 |
Ligands and binding sites
- 7LE · (5Z,8Z,11Z,14R,15R,17Z)-14,15-dihydroxyicosa-5,8,11,17-tetraenoic acid · 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, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 617 | 0.80 | 0.86 | 77 | empty |
| 2 | 383 | 0.77 | 0.87 | 63 | empty |
| 3 | 205 | 0.70 | 0.86 | 33 | 7LE |
| 4 | 320 | 0.68 | 0.82 | 44 | 7LE |
| 5 | 299 | 0.66 | 0.82 | 49 | 7LE |
Interfaces
5 interfaces between chains.
- C–D · 1423 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1421 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 633 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 620 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 485 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent, 4 disulfide (covalent ligand, disulfide).
Compared structures
- 5TNG · Crystal structure of the E153Q mutant of the CFTR inhibitory factor Cif containing the… · 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 A0A0M3KL26
- Elsewhere: RCSB PDB 5TNG · PDBe 5TNG · UniProt A0A0M3KL26
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