MolNFT v1 · #31954 · protein
Human DELTAF508 NBD1 with two solublizing mutations.
2BBT · Cystic fibrosis transmembrane conductance regulator: “Human DELTAF508 NBD1 with two solublizing mutations.”. X-ray diffraction, 2 ligands (ATP, MG), 3 pockets (best druggability 0.73). MolNFT v1 #31954 on GenesisL1: 3D structure…
- PDB
- 2BBT
- Type
- protein
- Length
- 507 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cystic fibrosis transmembrane conductance regulator
- UniProt
- P13569
- Ligands
- ATP, MG
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cystic fibrosis transmembrane conductance regulator | protein | 249 | 41% helix, 23% strand | P13569 |
| B | Cystic fibrosis transmembrane conductance regulator | protein | 258 | 40% helix, 22% 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
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 807 | 0.73 | 0.79 | 75 | MG, ATP |
| 2 | 132 | 0.45 | 0.77 | 36 | MG |
| 3 | 88 | 0.42 | 0.78 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 178 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2BBT · Human deltaF508 NBD1 with two solublizing mutations. · 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 0.94
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 2BBT · PDBe 2BBT · UniProt P13569
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.