MolNFT v1 · #168304 · protein
Human cftr first nucleotide binding domain with DF508/V510D
6WBS · Cystic fibrosis transmembrane conductance regulator: “Human cftr first nucleotide binding domain with DF508/V510D”. X-ray diffraction, 2 ligands (ATP, MG), 4 pockets (best druggability 0.70). MolNFT v1 #168304 on GenesisL1: 3D…
- PDB
- 6WBS
- Type
- protein
- Length
- 440 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cystic fibrosis transmembrane conductance regulator
- EC
- 5.6.1.6
- UniProt
- P13569
- Ligands
- ATP, MG
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cystic fibrosis transmembrane conductance regulator (EC 5.6.1.6) | protein | 215 | 33% helix, 28% strand | P13569 |
| B | Cystic fibrosis transmembrane conductance regulator (EC 5.6.1.6) | protein | 225 | 37% helix, 27% strand | P13569 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 778 | 0.70 | 0.77 | 74 | empty |
| 2 | 236 | 0.47 | 0.73 | 32 | empty |
| 3 | 105 | 0.36 | 0.75 | 22 | empty |
| 4 | 71 | 0.30 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 498 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 6WBS · Human CFTR first nucleotide binding domain with dF508/V510D · 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 0.96
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 6WBS · PDBe 6WBS · UniProt P13569
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.