› 4kkd

X-ray diffraction
2.6Å resolution

The X-ray crystal structure of Mannose-binding lectin-associated serine proteinase-3 reveals the structural basis for enzyme inactivity associated with the 3MC syndrome

Released:
DOI: 10.2210/pdb4kkd/pdb
PDB entry 4kkd coloured by chain, front view.
PDB entry 4kkd coloured by chain, side view.
PDB entry 4kkd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The x-ray crystal structure of mannose-binding lectin-associated serine proteinase-3 reveals the structural basis for enzyme inactivity associated with the Carnevale, Mingarelli, Malpuech, and Michels (3MC) syndrome.
Yongqing T, Wilmann PG, Reeve SB, Coetzer TH, Smith AI, Whisstock JC, Pike RN, Wijeyewickrema LC
J Biol Chem 288 22399-407 (2013)
PMID: 23792966

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155803 (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: 433 amino acids
Theoretical weight: 48.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P48740 (Residues: 298-443, 444-466, 467-469, 470-509, 510-574, 575-590, 591-624, 625-669, 670-697; Coverage: 58%)
Gene names: CRARF, CRARF1, MASP1, PRSS5
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand IMD 1 x IMD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P21212
Unit cell:
a: 72.84Å b: 292.916Å c: 43.589Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.26
Expression system: Escherichia coli

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Citations

8 review citations

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

6 mentions without citation

Alternatively Spliced Homologous Exons Have Ancient Origins and Are Highly Expressed at the Protein Level.
Abascal et al. (2015)
5 more