› 1pml

X-ray diffraction
2.38Å resolution

KRINGLE-KRINGLE INTERACTIONS IN MULTIMER KRINGLE STRUCTURES

Released:
DOI: 10.2210/pdb1pml/pdb
PDB entry 1pml coloured by chain, front view.
PDB entry 1pml coloured by chain, side view.
PDB entry 1pml 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: 
Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.
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-133299 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tissue-type plasminogen activator chain A Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 86 amino acids
Theoretical weight: 9.48 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00750 (Residues: 213-298; Coverage: 16%)
Gene name: PLAT
Sequence domains: Kringle domain
Structure domains: Plasminogen Kringle 4

Ligands and Environments

1 bound ligand:
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 54.8Å b: 63.58Å c: 46.58Å
α: 90° β: 106.7° γ: 90°
R-values:
R R work R free
0.145 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

4 mentions without citation

Plasminogen substrate recognition by the streptokinase-plasminogen catalytic complex is facilitated by Arg253, Lys256, and Lys257 in the streptokinase beta-domain and kringle 5 of the substrate.
Tharp et al. (2009)
3 more