› 1krn

X-ray diffraction
1.67Å resolution

STRUCTURE OF KRINGLE 4 AT 4C TEMPERATURE AND 1.67 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1krn/pdb
PDB entry 1krn coloured by chain, front view.
PDB entry 1krn coloured by chain, side view.
PDB entry 1krn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human plasminogen kringle 4 at 1.68 a and 277 K. A possible structural role of disordered residues.
Stec B, Yamano A, Whitlow M, Teeter MM
Acta Crystallogr D Biol Crystallogr 53 169-78 (1997)
PMID: 15299951

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.
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-133230 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Angiostatin Chain: A
Molecule details ›
Chain: A
Length: 88 amino acids
Theoretical weight: 9.9 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00747 (Residues: 374-461; Coverage: 11%)
Gene name: PLG
Sequence domains: Kringle domain
Structure domains: Plasminogen Kringle 4

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 49.44Å b: 50.27Å c: 32.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 0.147 0.232

Quick links

Citations

5 citation in other articles

The X-ray crystal structure of full-length human plasminogen.
Law et al. (2012)
4 more

11 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
10 more