PDBe 3gd7

X-ray diffraction
2.7Å resolution

Crystal structure of human NBD2 complexed with N6-Phenylethyl-ATP (P-ATP)

Released:
Entry authors: Atwell S, Antonysamy S, Conners K, Emtage S, Gheyi T, Lewis HA, Lu F, Sauder JM, Wasserman SR, Zhao X

Function and Biology Details

Reactions catalysed:
ATP + H(2)O + maltose-[maltose-binding protein](Side 1) = ADP + phosphate + maltose(Side 2) + [maltose-binding protein](Side 1)
ATP + H(2)O + closed Cl(-) channel = ADP + phosphate + open Cl(-) channel
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cystic fibrosis transmembrane conductance regulator; Maltose/maltodextrin import ATP-binding protein MalK Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 390 amino acids
Theoretical weight: 43.52 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P13569 (Residues: 1193-1410, 1412-1427; Coverage: 16%)
  • Canonical: P68187 (Residues: 202-202, 219-371; Coverage: 42%)
Gene names: ABCC7, CFTR, JW3995, b4035, malK
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21212
Unit cell:
a: 137.837Å b: 173.725Å c: 82.574Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.247 0.247 0.308
Expression system: Escherichia coli