MolNFT v1 · #27289 · protein
Structure of NBD1 from murine cftr- F508R mutant
1XFA · Cystic fibrosis transmembrane conductance regulator: “Structure of NBD1 from murine cftr- F508R mutant”. X-ray diffraction, 3 ligands (ATP, MG, CL), 6 pockets (best druggability 0.65). MolNFT v1 #27289 on GenesisL1: 3D structure…
- PDB
- 1XFA
- Type
- protein
- Length
- 528 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cystic fibrosis transmembrane conductance regulator
- UniProt
- P26361
- Ligands
- ATP, MG, CL
- Pockets
- 6 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cystic fibrosis transmembrane conductance regulator | protein | 264 | 42% helix, 23% strand | P26361 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A
- ACY · Acetic acid · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 396 | 0.65 | 0.79 | 60 | MG, ATP |
| 2 | 212 | 0.52 | 0.77 | 42 | MG, ATP |
| 3 | 193 | 0.50 | 0.77 | 20 | empty |
| 4 | 74 | 0.31 | 0.74 | 18 | empty |
| 5 | 55 | 0.30 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 806 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 1XFA · Structure of NBD1 from murine CFTR- F508R mutant · the same entry in another collection · chain A against A, TM-score 1.00
- P26361 · AlphaFold monomer V2.0 prediction for cystic fibrosis transmembrane conductance regulator… · a predicted model of the same protein · chain B against A, TM-score 0.91
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 P26361
- Elsewhere: RCSB PDB 1XFA · PDBe 1XFA · UniProt P26361
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