› 1kiv

X-ray diffraction
2.1Å resolution

RECOMBINANT KRINGLE IV-10/M66 VARIANT OF HUMAN APOLIPOPROTEIN(A)

Released:
DOI: 10.2210/pdb1kiv/pdb
PDB entry 1kiv coloured by chain, front view.
PDB entry 1kiv coloured by chain, side view.
PDB entry 1kiv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Recombinant kringle IV-10 modules of human apolipoprotein(a): structure, ligand binding modes, and biological relevance.
Mochalkin I, Cheng B, Klezovitch O, Scanu AM, Tulinsky A
Biochemistry 38 1990-8 (1999)
PMID: 10026282

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: 78 amino acids
Theoretical weight: 9.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08519 (Residues: 1616-1693; Coverage: 4%)
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
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 24.61Å b: 45.68Å c: 63.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

What the structure of angiostatin may tell us about its mechanism of action.
Geiger et al. (2004)
1 more

4 mentions without citation

A conservation and rigidity based method for detecting critical protein residues.
Akbal-Delibas et al. (2013)
3 more