MolNFT v1 · #135823 · protein
Dephosphorylated, ATP-free human cystic fibrosis transmembrane conductance regulator (cftr)
5UAK: “Dephosphorylated, ATP-free human cystic fibrosis transmembrane conductance regulator (cftr)”. Electron microscopy, 20 pockets (best druggability 0.82). MolNFT v1 #135823 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5UAK
- Type
- protein
- Length
- 1,158 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cystic fibrosis transmembrane conductance regulator
- EC
- 3.6.3.49
- UniProt
- P13569
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 2 distinct chains · 63% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cystic fibrosis transmembrane conductance regulator (EC 3.6.3.49) | protein | 1139 | 63% helix, 9% strand | P13569 |
| R | Cystic fibrosis transmembrane conductance regulator | protein | 19 | 63% helix, 0% strand | — |
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 836 | 0.82 | 0.84 | 69 | empty |
| 2 | 130 | 0.77 | 0.95 | 29 | empty |
| 3 | 290 | 0.76 | 0.88 | 48 | empty |
| 4 | 96 | 0.74 | 0.95 | 29 | empty |
| 5 | 592 | 0.73 | 0.80 | 63 | empty |
Interfaces
1 interface between chains.
- A–R · 668 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 5UAK · Dephosphorylated, ATP-free human cystic fibrosis transmembrane conductance regulator… · the same entry in another collection · chain A against A, TM-score 1.00
- P13569 · AlphaFold monomer V2.0 prediction for cystic fibrosis transmembrane conductance regulator… · a predicted model of the same protein · chain A against A, TM-score 0.83
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 P13569
- Elsewhere: RCSB PDB 5UAK · PDBe 5UAK · UniProt P13569
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