› 1q3x

X-ray diffraction
2.23Å resolution

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
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126140 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mannan-binding lectin serine protease 2 A chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 328 amino acids
Theoretical weight: 35.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O00187 (Residues: 363-686; Coverage: 48%)
Gene name: MASP2
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand NA 2 x NA
Ligand GOL 7 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P1
Unit cell:
a: 40.95Å b: 41.521Å c: 102.994Å
α: 96.44° β: 91.77° γ: 119.52°
R-values:
R R work R free
0.176 0.174 0.224
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

18 review citations

Complement and its role in innate and adaptive immune responses.
Dunkelberger et al. (2010)
17 more

8 mentions without citation

Monospecific inhibitors show that both mannan-binding lectin-associated serine protease-1 (MASP-1) and -2 Are essential for lectin pathway activation and reveal structural plasticity of MASP-2.
Héja et al. (2012)
7 more