› 1pk4

X-ray diffraction
1.9Å resolution

CRYSTAL AND MOLECULAR STRUCTURE OF HUMAN PLASMINOGEN KRINGLE 4 REFINED AT 1.9-ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1pk4/pdb
PDB entry 1pk4 coloured by chain, front view.
PDB entry 1pk4 coloured by chain, side view.
PDB entry 1pk4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal and molecular structure of human plasminogen kringle 4 refined at 1.9-A resolution.
Mulichak AM, Tulinsky A, Ravichandran KG
Biochemistry 30 10576-88 (1991)
PMID: 1657148

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: 79 amino acids
Theoretical weight: 9.04 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00747 (Residues: 376-454; Coverage: 10%)
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: 32.11Å b: 49.09Å c: 49.39Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.142 not available not available
Expression system: Not provided

Quick links

Citations

11 review citations

A player of many parts: the spotlight falls on thrombin's structure.
Stubbs et al. (1993)
10 more

2 mentions without citation

High-resolution crystal structure of apolipoprotein(a) kringle IV type 7: insights into ligand binding.
Ye et al. (2001)
1 more