› 1pmk

X-ray diffraction
2.25Å resolution

KRINGLE-KRINGLE INTERACTIONS IN MULTIMER KRINGLE STRUCTURES

Released:
DOI: 10.2210/pdb1pmk/pdb
PDB entry 1pmk coloured by chain, front view.
PDB entry 1pmk coloured by chain, side view.
PDB entry 1pmk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Kringle-kringle interactions in multimer kringle structures.
Padmanabhan K, Wu TP, Ravichandran KG, Tulinsky A
Protein Sci 3 898-910 (1994)
PMID: 8069221

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 88 amino acids
Theoretical weight: 9.9 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00747 (Residues: 374-461; Coverage: 11%)
Gene name: PLG
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
Spacegroup: P21
Unit cell:
a: 32.73Å b: 49.09Å c: 46.15Å
α: 90° β: 100.6° γ: 90°
R-values:
R R work R free
0.165 not available not available
Expression system: Not provided

Quick links

Citations

2 review citations

Coagulation factors and their inhibitors.
Stubbs et al. (1994)
1 more

2 mentions without citation

Type III secretion system effector proteins are mechanically labile.
LeBlanc et al. (2021)
1 more