› 1xf9

X-ray diffraction
2.7Å resolution

Structure of NBD1 from murine CFTR- F508S mutant

Released:
DOI: 10.2210/pdb1xf9/pdb
PDB entry 1xf9 coloured by chain, front view.
PDB entry 1xf9 coloured by chain, side view.
PDB entry 1xf9 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Side chain and backbone contributions of Phe508 to CFTR folding.
Thibodeau PH, Brautigam CA, Machius M, Thomas PJ
Nat Struct Mol Biol 12 10-6 (2005)
PMID: 15619636

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + closed Cl(-) channel = ADP + phosphate + open Cl(-) channel
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo hexamer
homo octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-150714 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cystic fibrosis transmembrane conductance regulator Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 283 amino acids
Theoretical weight: 31.71 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P26361 (Residues: 389-670; Coverage: 19%)
Gene names: Abcc7, Cftr
Sequence domains: ABC transporter
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand MG 7 x MG
Ligand ATP 4 x ATP
Ligand ACY 6 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P4212
Unit cell:
a: 170.449Å b: 170.449Å c: 109.065Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.201 0.253
Expression system: Escherichia coli

Quick links

Citations

23 review citations

The ABC protein turned chloride channel whose failure causes cystic fibrosis.
Gadsby et al. (2006)
22 more

5 mentions without citation

Cystic fibrosis transmembrane conductance regulator (ABCC7) structure.
Hunt et al. (2013)
4 more