› 2feb

Solution NMR

NMR Solution Structure, Dynamics and Binding Properties of the Kringle IV Type 8 module of apolipoprotein(a)

Released:
DOI: 10.2210/pdb2feb/pdb
PDB entry 2feb coloured by chain, ensemble of 20 models, front view.
PDB entry 2feb coloured by chain, ensemble of 20 models, side view.
PDB entry 2feb coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Nuclear magnetic resonance (NMR) solution structure, dynamics, and binding properties of the kringle IV type 8 module of apolipoprotein(a).
Chitayat S, Kanelis V, Koschinsky ML, Smith SP
Biochemistry 46 1732-42 (2007)
PMID: 17263558

Function and Biology Details

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

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: 102 amino acids
Theoretical weight: 11.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08519 (Residues: 1377-1472; 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: simulated annealing molecular dynamics torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

NMR backbone dynamics of VEK-30 bound to the human plasminogen kringle 2 domain.
Wang et al. (2010)
1 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