› 1b0q

Solution NMR

DITHIOL ALPHA MELANOTROPIN PEPTIDE CYCLIZED VIA RHENIUM METAL COORDINATION

Released:
DOI: 10.2210/pdb1b0q/pdb
PDB entry 1b0q coloured by chain, front view.
PDB entry 1b0q coloured by chain, side view.
PDB entry 1b0q coloured by chain, top view.
Source organism: Synthetic construct
Primary publication:
Design and characterization of alpha-melanotropin peptide analogs cyclized through rhenium and technetium metal coordination.
Giblin MF, Wang N, Hoffman TJ, Jurisson SS, Quinn TP
Proc Natl Acad Sci U S A 95 12814-8 (1998)
PMID: 9788997

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-162113 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PROTEIN (CYCLIC ALPHA MELANOCYTE STIMULATING HORMONE) Chain: A
Molecule details ›
Chain: A
Length: 12 amino acids
Theoretical weight: 1.33 KDa
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand RE 1 x RE
1 modified residue:
Ligand DPN 1 x DPN

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

18 review citations

Target-specific delivery of peptide-based probes for PET imaging.
Chen et al. (2010)
17 more

2 mentions without citation

Trends in coordination of rhenium organometallic complexes in the Protein Data Bank.
Brink et al. (2022)
1 more