› 4igd

X-ray diffraction
2.5Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155803 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mannan-binding lectin serine protease 1 heavy chain Chain: A
Molecule details ›
Chain: A
Length: 406 amino acids
Theoretical weight: 45.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P48740 (Residues: 298-699; Coverage: 59%)
Gene names: CRARF, CRARF1, MASP1, PRSS5
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 63.31Å b: 69.61Å c: 117.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.219 0.248
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Complement System Part I - Molecular Mechanisms of Activation and Regulation.
Merle et al. (2015)
14 more

4 mentions without citation

Quantitative characterization of the activation steps of mannan-binding lectin (MBL)-associated serine proteases (MASPs) points to the central role of MASP-1 in the initiation of the complement lectin pathway.
Megyeri et al. (2013)
3 more