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X-ray diffraction
2.55Å resolution

Crystal structure of the catalytic region of human MASP-1

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-155804 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mannan-binding lectin serine protease 1 heavy chain Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 17.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P48740 (Residues: 298-448; Coverage: 22%)
Gene names: CRARF, CRARF1, MASP1, PRSS5
Sequence domains: Sushi repeat (SCR repeat)
Structure domains: Complement Module, domain 1
Mannan-binding lectin serine protease 1 light chain Chain: B
Molecule details ›
Chain: B
Length: 251 amino acids
Theoretical weight: 28.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P48740 (Residues: 449-699; Coverage: 37%)
Gene names: CRARF, CRARF1, MASP1, PRSS5
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 68.418Å b: 70.412Å c: 121.413Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.229 0.278
Expression system: Escherichia coli