› 1jfn

Solution NMR

SOLUTION STRUCTURE OF HUMAN APOLIPOPROTEIN(A) KRINGLE IV TYPE 6

Released:
DOI: 10.2210/pdb1jfn/pdb
PDB entry 1jfn coloured by chain, ensemble of 15 models, front view.
PDB entry 1jfn coloured by chain, ensemble of 15 models, side view.
PDB entry 1jfn coloured by chain, ensemble of 15 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of human apolipoprotein(a) kringle IV type 6.
Maderegger B, Bermel W, Hrzenjak A, Kostner GM, Sterk H
Biochemistry 41 660-8 (2002)
PMID: 11781107

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140162 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apolipoprotein(a) Chain: A
Molecule details ›
Chain: A
Length: 119 amino acids
Theoretical weight: 13.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08519 (Residues: 1157-1262; Coverage: 5%)
Gene name: LPA
Sequence domains: Kringle domain
Structure domains: Plasminogen Kringle 4

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry, simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Structure-function relationships in apolipoprotein(a): insights into lipoprotein(a) assembly and pathogenicity.
Koschinsky et al. (2004)
2 more

2 mentions 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)
1 more