1ki0

X-ray diffraction
1.75Å resolution

The X-ray Structure of Human Angiostatin

Released:

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

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: 253 amino acids
Theoretical weight: 29.08 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P00747 (Residues: 100-352; Coverage: 32%)
Gene name: PLG
Sequence domains: Kringle domain
Structure domains: Plasminogen Kringle 4

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P41212
Unit cell:
a: 56.943Å b: 56.943Å c: 192.966Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.263
Expression system: Komagataella pastoris