Research workbench
Dephosphorylated, ATP-free cystic fibrosis transmembrane conductance regulator (cftr) from zebrafish
Analyse Dephosphorylated, ATP-free cystic fibrosis transmembrane conductance regulator… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UAR
- Type
- protein
- Length
- 1,184 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cystic fibrosis transmembrane conductance regulator
- EC
- 3.6.3.49
- UniProt
- Q1LX78
- Ligands
- D10
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 1 distinct chain · 61% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cystic fibrosis transmembrane conductance regulator (EC 3.6.3.49) | protein | 1184 | 61% helix, 6% strand | Q1LX78 |
Ligands and binding sites
- D10 · Decane · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1182 | 0.78 | 0.80 | 75 | empty |
| 2 | 193 | 0.77 | 0.92 | 40 | empty |
| 3 | 285 | 0.76 | 0.88 | 29 | empty |
| 4 | 103 | 0.73 | 0.94 | 26 | empty |
| 5 | 120 | 0.71 | 0.91 | 29 | empty |
Compared structures
- 5UAR · Dephosphorylated, ATP-free cystic fibrosis transmembrane conductance regulator (CFTR)… · the same entry in another collection · chain A against A, TM-score 1.00
- Q1LX78 · AlphaFold monomer V2.0 prediction for cystic fibrosis transmembrane conductance regulator… · a predicted model of the same protein · chain A against A, TM-score 0.79
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 Q1LX78
- Elsewhere: RCSB PDB 5UAR · PDBe 5UAR · UniProt Q1LX78
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