› 3poj

X-ray diffraction
1.45Å resolution

Crystal structure of MASP-1 CUB2 domain bound to Ethylamine

Released:
DOI: 10.2210/pdb3poj/pdb
PDB entry 3poj coloured by chain, front view.
PDB entry 3poj coloured by chain, side view.
PDB entry 3poj 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

Assemblies composition:
monomeric (preferred)
homo hexamer
homo trimer
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
Molecule details ›
Chains: A, B
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

4 bound ligands:
Ligand CA 2 x CA
Ligand NEH 1 x NEH
Ligand SO4 2 x SO4
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P213
Unit cell:
a: 100.48Å b: 100.48Å c: 100.48Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.126 0.125 0.155
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

1 mention without citation

Leishmania donovani tyrosyl-tRNA synthetase structure in complex with a tyrosyl adenylate analog and comparisons with human and protozoan counterparts.
Barros-Álvarez et al. (2017)