Calcium in PDB 8uw8: Site-One Protease and Spring

The binding sites of Calcium atom in the Site-One Protease and Spring (pdb code 8uw8). 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 Site-One Protease and Spring, PDB code: 8uw8:

Calcium binding site 1 out of 1 in the Site-One Protease and Spring


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Site-One Protease and Spring within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1102 b:30.1 occ:1.00 H1 A:HOH1209 2.1 37.7 1.0 H2 A:HOH1209 2.1 38.9 1.0 O A:ASP697 2.2 39.6 1.0 OE1 A:GLU699 2.4 33.0 1.0 OD1 A:ASN630 2.4 44.5 1.0 O A:HOH1209 2.4 38.2 1.0 HB3 A:ASP697 2.7 36.5 1.0 O A:HOH1201 2.7 28.4 1.0 H2 A:HOH1201 3.0 34.8 1.0 OE2 A:GLU699 3.0 59.2 1.0 CD A:GLU699 3.1 39.4 1.0 OD2 A:ASP697 3.1 31.4 1.0 C A:ASP697 3.3 38.1 1.0 CB A:ASP697 3.5 25.7 1.0 CG A:ASN630 3.5 32.6 1.0 H1 A:HOH1201 3.5 33.7 1.0 OD2 A:ASP651 3.6 39.7 1.0 OD2 A:ASP655 3.6 53.7 1.0 CG A:ASP697 3.6 25.9 1.0 HA A:ASN630 3.7 37.8 1.0 CG A:ASP655 3.7 47.8 1.0 H A:LEU631 3.9 39.1 1.0 O A:LEU631 3.9 47.8 1.0 CA A:ASP697 4.0 33.6 1.0 OD1 A:ASP655 4.0 50.9 1.0 O A:VAL696 4.0 47.2 1.0 HB2 A:ASN630 4.0 38.0 1.0 HA A:SER698 4.1 39.3 1.0 HB3 A:ASP655 4.1 40.2 1.0 HB2 A:ASP655 4.1 39.9 1.0 CB A:ASN630 4.2 39.2 1.0 H A:GLU699 4.3 39.7 1.0 HB2 A:ASP697 4.3 32.9 1.0 CB A:ASP655 4.3 39.1 1.0 CA A:ASN630 4.4 34.3 1.0 N A:SER698 4.4 37.6 1.0 N A:LEU631 4.5 31.4 1.0 ND2 A:ASN630 4.5 30.7 1.0 CG A:GLU699 4.6 41.3 1.0 HD22 A:ASN630 4.6 35.9 1.0 HB2 A:GLU699 4.7 40.8 1.0 CA A:SER698 4.7 34.3 1.0 OD1 A:ASP697 4.7 44.0 1.0 HA A:ASP697 4.7 35.8 1.0 N A:GLU699 4.7 30.0 1.0 CG A:ASP651 4.8 36.9 1.0 C A:VAL696 4.9 42.1 1.0 HB3 A:ARG632 4.9 39.6 1.0 C A:ASN630 4.9 38.0 1.0 N A:ASP697 4.9 31.9 1.0 C A:LEU631 4.9 36.4 1.0

S.Hendrix, V.Dartigue, H.Hall, S.Bawaria, J.Kingma, B.Bajaj, N.Zelcer, D.L.Kober. Spring Licenses S1P-Mediated Cleavage of SREBP2 By Displacing An Inhibitory Pro-Domain Nat Commun 2024.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-024-50068-8