MolNFT v1 · #89374 · protein
Crystal structure of the cftr inhibitory factor cif with the E153Q mutation adducted with the epibromohydrin hydrolysis intermediate
4DNF · Putative hydrolase: “Crystal structure of the cftr inhibitory factor cif with the E153Q mutation adducted with the epibromohydrin…”. X-ray diffraction, 1 ligand (EBH), 10 pockets (best druggability 0.81). MolNFT v1 #89374 on…
- PDB
- 4DNF
- Type
- protein
- Length
- 1,184 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative hydrolase
- UniProt
- Q02P97
- Ligands
- EBH
- Pockets
- 10 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Putative hydrolase | protein | 296 | 43% helix, 18% strand | Q02P97 |
Ligands and binding sites
- EBH · (2S)-1-bromopropan-2-ol · 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, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 296 | 0.81 | 0.92 | 46 | empty |
| 2 | 306 | 0.79 | 0.91 | 52 | empty |
| 3 | 50 | 0.70 | 0.98 | 19 | EBH |
| 4 | 237 | 0.62 | 0.81 | 27 | empty |
| 5 | 230 | 0.61 | 0.81 | 30 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1428 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 1407 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 657 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 647 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 487 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent, 4 disulfide (covalent ligand, disulfide).
Compared structures
- 4DNF · Crystal structure of the CFTR inhibitory factor Cif with the E153Q mutation adducted with… · 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 Q02P97
- Elsewhere: RCSB PDB 4DNF · PDBe 4DNF · UniProt Q02P97
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