5ubm

X-ray diffraction
2.5Å resolution

Crystal structure of human C1s in complex with inhibitor gigastasin

Released:

Function and Biology Details

Reaction catalysed:
Cleavage of Arg-|-Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)-|-Lys bond in complement component C2 to form C2a and C2b: the 'classical' pathway C3 convertase.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-140781 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
Complement C1s subcomponent light chain Chain: A
Molecule details ›
Chain: A
Length: 252 amino acids
Theoretical weight: 27.84 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P09871 (Residues: 437-688; Coverage: 37%)
Gene name: C1S
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Complement C1s subcomponent heavy chain Chain: B
Molecule details ›
Chain: B
Length: 152 amino acids
Theoretical weight: 16.88 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P09871 (Residues: 285-436; Coverage: 23%)
Gene name: C1S
Sequence domains: Sushi repeat (SCR repeat)
Structure domains: Complement Module, domain 1
Gigastasin Chain: I
Molecule details ›
Chain: I
Length: 137 amino acids
Theoretical weight: 16.1 KDa
Source organism: Haementeria ghilianii
Expression system: Trichoplusia ni

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P3121
Unit cell:
a: 89.35Å b: 89.35Å c: 146.871Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.177 0.222
Expression system: Trichoplusia ni