› 3pog

X-ray diffraction
2.75Å resolution

Crystal structure of the MASP-1 CUB2 domain bound to Ca2+

Released:
DOI: 10.2210/pdb3pog/pdb
PDB entry 3pog coloured by chain, front view.
PDB entry 3pog coloured by chain, side view.
PDB entry 3pog 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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183967 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mannan-binding lectin serine protease 1 heavy chain Chains: A, B, C
Molecule details ›
Chains: A, B, C
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

Ligands and Environments

1 bound ligand:
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 111.68Å b: 64.69Å c: 52.42Å
α: 90° β: 92.33° γ: 90°
R-values:
R R work R free
0.236 0.233 0.286
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

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

8 mentions without citation

Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.
Ernst et al. (2014)
7 more