1ddj

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF HUMAN PLASMINOGEN CATALYTIC DOMAIN

Released:

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: 247 amino acids
Theoretical weight: 27.08 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00747 (Residues: 564-810; 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 X12C
Spacegroup: P21
Unit cell:
a: 90.49Å b: 46.16Å c: 126.65Å
α: 90° β: 91.75° γ: 90°
R-values:
R R work R free
0.194 0.194 0.267
Expression system: Escherichia coli