› 4iw4

X-ray diffraction
3.2Å resolution

Crystal structure of the serine protease domain of MASP-3 in complex with ecotin

Released:
DOI: 10.2210/pdb4iw4/pdb
PDB entry 4iw4 coloured by chain, front view.
PDB entry 4iw4 coloured by chain, side view.
PDB entry 4iw4 coloured by chain, top view.
Source organisms:
Primary publication:
The serine protease domain of MASP-3: enzymatic properties and crystal structure in complex with ecotin.
Gaboriaud C, Gupta RK, Martin L, Lacroix M, Serre L, Teillet F, Arlaud GJ, Rossi V, Thielens NM
PLoS One 8 e67962 (2013)
PMID: 23861840

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
hetero octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-150068 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ecotin Chains: C, D
Molecule details ›
Chains: C, D
Length: 142 amino acids
Theoretical weight: 16.12 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P23827 (Residues: 21-162; Coverage: 100%)
Gene names: JW2197, b2209, eco, eti
Sequence domains: Ecotin
Structure domains: Ecotin
Mannan-binding lectin serine protease 1 light chain Chains: E, F
Molecule details ›
Chains: E, F
Length: 279 amino acids
Theoretical weight: 30.58 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P48740 (Residues: 449-466, 467-469, 470-509, 510-574, 575-590, 591-624, 625-669, 670-697; Coverage: 35%)
Gene names: CRARF, CRARF1, MASP1, PRSS5
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1, ESRF BEAMLINE ID14-2, ESRF BEAMLINE ID29, ESRF BEAMLINE BM14
Spacegroup: P21212
Unit cell:
a: 66.72Å b: 164.62Å c: 90.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.269
Expression system: Trichoplusia ni

Quick links

Citations

4 review citations

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

3 mentions without citation

MASP-3 is the exclusive pro-factor D activator in resting blood: the lectin and the alternative complement pathways are fundamentally linked.
Dobó et al. (2016)
2 more