1zjk

X-ray diffraction
2.18Å resolution

Crystal structure of the zymogen catalytic region of human MASP-2

Released:

Function and Biology Details

Reaction catalysed:
Selective cleavage after Arg(223) in complement component C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg(76) in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-126140 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mannan-binding lectin serine protease 2 A chain Chain: A
Molecule details ›
Chain: A
Length: 403 amino acids
Theoretical weight: 44.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O00187 (Residues: 287-686; Coverage: 60%)
Gene name: MASP2
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 47.665Å b: 72.689Å c: 110.989Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.205 0.253
Expression system: Escherichia coli BL21(DE3)