PDBe 4c3z

X-ray diffraction
2.1Å resolution

Nucleotide-free crystal structure of nucleotide-binding domain 1 from human MRP1 supports a general-base catalysis mechanism for ATP hydrolysis.

Released:

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multidrug resistance-associated protein 1 Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 29.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P33527 (Residues: 628-881; Coverage: 17%)
Gene names: ABCC1, MRP, MRP1
Sequence domains: ABC transporter
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P31
Unit cell:
a: 64.299Å b: 64.299Å c: 65.491Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.164 0.194
Expression system: Escherichia coli BL21(DE3)