1qrz

X-ray diffraction
2Å resolution

CATALYTIC DOMAIN OF PLASMINOGEN

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of the proenzyme domain of plasminogen.
Biochemistry 38 11180-8 (1999)
PMID: 10460175

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133230 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Plasmin light chain B Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 246 amino acids
Theoretical weight: 27.02 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00747 (Residues: 565-810; Coverage: 31%)
Gene name: PLG
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P21
Unit cell:
a: 81.658Å b: 73.575Å c: 81.363Å
α: 90° β: 108.73° γ: 90°
R-values:
R R work R free
0.237 0.235 0.294
Expression system: Not provided