› 2ls2

Solution NMR

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

Released:
DOI: 10.2210/pdb2ls2/pdb
PDB entry 2ls2 coloured by chain, ensemble of 20 models, front view.
PDB entry 2ls2 coloured by chain, ensemble of 20 models, side view.
PDB entry 2ls2 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into the transmembrane domains of human copper transporter 1.
Yang L, Huang Z, Li F
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)
Assembly name:
PDBe Complex ID:
PDB-CPX-127470 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Truncated CTR1 form 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: 49%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

How copper traverses cellular membranes through the mammalian copper transporter 1, Ctr1.
Ohrvik et al. (2014)
1 more

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)