Zymogen and activated protein C have similar structural architecture.

Stojanovski BM, Pelc LA, Zuo X, Di Cera E, J Biol Chem (2020) Europe PMC

SASDJC6 – Human Vitamin K-dependent protein C

Vitamin K-dependent protein C
MWexperimental 62 kDa
MWexpected 62 kDa
log I(s) 9.10×10-2 9.10×10-3 9.10×10-4 9.10×10-5
Vitamin K-dependent protein C small angle scattering data  s, nm-1
ln I(s)
Vitamin K-dependent protein C Guinier plot ln 9.10×10-2 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Vitamin K-dependent protein C Kratky plot 1.104 0 √3 sRg
p(r)
Vitamin K-dependent protein C pair distance distribution function Rg: 3.7 nm 0 Dmax: 14 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Vitamin K-dependent protein C DAMFILT model
Vitamin K-dependent protein C DAMMIF model
Synchrotron SAXS data from solutions of Human Vitamin K-dependent protein C in 20 mM Tris, 145 mM NaCl, 5 mM CaCl2, pH 7.5 were collected on the 12-ID-B SAXS/WAXS beam line at the Advanced Photon Source (APS), Argonne National Laboratory storage ring (Lemont, IL, USA) using a Pilatus 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.09322 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 23°C. 45 successive 0.500 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Experimental MW adopted from Bayesian Inference method using ATSAS.

Vitamin K-dependent protein C (Protein C)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   62 kDa
 
UniProt   P04070 (43-461)
Sequence   FASTA