› 3pob

X-ray diffraction
1.8Å resolution

Crystal structure of MASP-1 CUB2 domain in complex with the collagen-like domain of MBL

Released:
DOI: 10.2210/pdb3pob/pdb
PDB entry 3pob coloured by chain, front view.
PDB entry 3pob coloured by chain, side view.
PDB entry 3pob coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structural basis of mannan-binding lectin recognition by its associated serine protease MASP-1: implications for complement activation.
Gingras AR, Girija UV, Keeble AH, Panchal R, Mitchell DA, Moody PC, Wallis R
Structure 19 1635-43 (2011)
PMID: 22078562

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163888 (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: 115 amino acids
Theoretical weight: 13.09 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8CHN8 (Residues: 188-301; Coverage: 17%)
Gene names: Crarf, Masp1, Masp3
Sequence domains: CUB domain
Structure domains: Spermadhesin, CUB domain
MBL collagen-like peptide Chains: B, C, D
Molecule details ›
Chains: B, C, D
Length: 29 amino acids
Theoretical weight: 2.48 KDa
Source organism: Rattus norvegicus
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
1 modified residue:
Ligand HYP 24 x HYP

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21212
Unit cell:
a: 61.2Å b: 52.56Å c: 57.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.252
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

12 review citations

Complement activation, regulation, and molecular basis for complement-related diseases.
Bajic et al. (2015)
11 more

8 mentions without citation

Polyproline and triple helix motifs in host-pathogen recognition.
Berisio et al. (2012)
7 more