2ls2

Solution NMR

1H Chemical Shift Assignments for the first transmembrane domain from human copper transport 1

Released:
Source organism: Homo sapiens
Primary publication:
Structural insights into the transmembrane domains of human copper transporter 1.
J. Pept. Sci. 18 449-55 (2012)
PMID: 22615137

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
High affinity copper uptake protein 1 Chain: A
Molecule details ›
Chain: A
Length: 25 amino acids
Theoretical weight: 2.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15431 (Residues: 64-87; Coverage: 13%)
Gene names: COPT1, CTR1, SLC31A1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 45%
Refinement method: torsion angle dynamics
Chemical shifts: BMR18408  
Expression system: Escherichia coli