Calcium in PDB 3bps: PCSK9:Egf-A Complex

The structure of PCSK9:Egf-A Complex, PDB code: 3bps was solved by H.J.Kwon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.41
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	116.952, 116.952, 134.878, 90.00, 90.00, 90.00
R / Rfree (%)	20.3 / 24

The binding sites of Calcium atom in the PCSK9:Egf-A Complex (pdb code 3bps). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the PCSK9:Egf-A Complex, PDB code: 3bps:

Calcium binding site 1 out of 1 in the PCSK9:Egf-A Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of PCSK9:Egf-A Complex within 5.0Å range: probe atom residue distance (Å) B Occ E:Ca1 b:47.0 occ:1.00 O E:HOH373 2.4 35.8 1.0 OD1 E:ASP310 2.4 46.7 1.0 O E:LEU311 2.4 40.8 1.0 O E:GLY314 2.5 43.5 1.0 O E:THR294 2.6 51.7 1.0 OE1 E:GLU296 2.6 47.0 1.0 O E:MET292 2.9 56.6 1.0 CD E:GLU296 3.4 47.9 1.0 OE2 E:GLU296 3.5 46.4 1.0 C E:GLY314 3.5 44.9 1.0 CG E:ASP310 3.5 46.9 1.0 C E:LEU311 3.6 41.0 1.0 C E:THR294 3.8 51.7 1.0 N E:GLY314 3.9 42.4 1.0 CA E:GLY314 4.0 43.3 1.0 N E:LEU311 4.0 43.5 1.0 C E:MET292 4.1 56.8 1.0 N E:THR294 4.1 53.6 1.0 OD2 E:ASP310 4.1 45.1 1.0 O E:LYS312 4.2 39.9 1.0 C E:LYS312 4.3 40.0 1.0 C E:ASP310 4.4 44.9 1.0 CA E:LEU311 4.4 41.8 1.0 N E:LYS312 4.6 40.4 1.0 N E:GLU296 4.6 50.0 1.0 CA E:ASN295 4.6 50.3 1.0 N E:ASN295 4.6 51.0 1.0 CA E:ASP310 4.6 45.6 1.0 CA E:LYS312 4.6 39.9 1.0 C E:ILE313 4.7 41.5 1.0 O E:HOH375 4.7 56.4 1.0 N E:TYR315 4.7 46.2 1.0 CA E:THR294 4.7 52.2 1.0 CB E:ASP310 4.7 46.1 1.0 N E:ILE313 4.8 40.6 1.0 C E:GLY293 4.9 54.8 1.0 CG E:GLU296 4.9 47.9 1.0 CA E:GLY293 4.9 55.5 1.0 O A:HOH106 4.9 64.8 1.0 N E:GLY293 4.9 56.2 1.0

H.J.Kwon, T.A.Lagace, M.C.Mcnutt, J.D.Horton, J.Deisenhofer. Molecular Basis For Ldl Receptor Recognition By PCSK9. Proc.Natl.Acad.Sci.Usa V. 105 1820 2008.
ISSN: ISSN 0027-8424
PubMed: 18250299
DOI: 10.1073/PNAS.0712064105