› 6rv6

X-ray diffraction
3.51Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151103 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (4 distinct):
Properdin Chain: A
Molecule details ›
Chain: A
Length: 170 amino acids
Theoretical weight: 18.64 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P27918 (Residues: 28-191; Coverage: 37%)
Gene names: CFP, PFC
Sequence domains:
Properdin Chain: B
Molecule details ›
Chain: B
Length: 221 amino acids
Theoretical weight: 24.72 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P27918 (Residues: 256-469; Coverage: 48%)
Gene names: CFP, PFC
Sequence domains: Thrombospondin type 1 domain

Ligands and Environments

Carbohydrate polymer : NEW Components: FUC, BGC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: FUC, NAG
Carbohydrate polymer
1 bound ligand:
Ligand MAN 12 x MAN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: I41
Unit cell:
a: 219.79Å b: 219.79Å c: 47.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.265 0.264 0.284
Expression system: Homo sapiens

Quick links

Citations

6 review citations

Meta-heterogeneity: Evaluating and Describing the Diversity in Glycosylation Between Sites on the Same Glycoprotein.
Čaval et al. (2021)
5 more

2 mentions without citation

Structural studies offer a framework for understanding the role of properdin in the alternative pathway and beyond.
Pedersen et al. (2023)
1 more