Calcium in PDB 1q1p: E-Cadherin Activation

The structure of E-Cadherin Activation, PDB code: 1q1p was solved by D.Haussinger, J.Stetefeld, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 3.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	129.204, 48.601, 58.669, 90.00, 113.93, 90.00
R / Rfree (%)	25.9 / 30.5

The binding sites of Calcium atom in the E-Cadherin Activation (pdb code 1q1p). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the E-Cadherin Activation, PDB code: 1q1p:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the E-Cadherin Activation


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of E-Cadherin Activation within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca701 b:19.5 occ:1.00 OD1 A:ASP100 2.1 19.9 1.0 OE2 A:GLU69 2.4 17.9 1.0 O A:GLN101 2.4 18.5 1.0 OE1 A:GLU69 2.6 30.4 1.0 CD A:GLU69 2.7 25.0 1.0 OD1 A:ASP103 2.9 31.2 1.0 OD1 A:ASP136 3.1 30.2 1.0 ND2 A:ASN104 3.1 23.6 1.0 CG A:ASP100 3.2 18.6 1.0 OE2 A:GLU11 3.3 26.7 1.0 OD2 A:ASP100 3.4 16.9 1.0 C A:GLN101 3.7 20.1 1.0 OE1 A:GLU11 3.7 24.4 1.0 CB A:ASP136 3.7 26.3 1.0 CA A:ASP136 3.8 25.9 1.0 CG A:ASP136 3.8 28.0 1.0 CD A:GLU11 3.9 25.7 1.0 CG A:ASP103 4.0 28.9 1.0 CG A:GLU69 4.0 24.0 1.0 N A:GLN101 4.0 18.2 1.0 N A:ASP103 4.3 25.3 1.0 OD2 A:ASP103 4.4 31.1 1.0 CG A:ASN104 4.4 22.5 1.0 CA A:GLN101 4.5 19.5 1.0 CB A:ASP100 4.5 18.4 1.0 CA A:CA703 4.6 30.9 1.0 N A:ASN102 4.6 22.4 1.0 CA A:ASN102 4.7 24.2 1.0 N A:ASP136 4.7 25.7 1.0 NE A:ARG68 4.8 26.2 1.0 C A:ASP136 4.9 25.2 1.0 N A:ASP137 4.9 24.4 1.0 CA A:ASP100 5.0 18.2 1.0 OD2 A:ASP136 5.0 30.1 1.0 C A:ASP100 5.0 18.0 1.0

Calcium binding site 2 out of 3 in the E-Cadherin Activation


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of E-Cadherin Activation within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca702 b:26.6 occ:1.00 OD2 A:ASP136 2.0 30.1 1.0 O A:ASN104 2.3 21.9 1.0 OD2 A:ASP195 2.4 16.5 1.0 OD1 A:ASN102 2.4 27.5 1.0 CG A:ASN102 2.9 26.8 1.0 ND2 A:ASN102 2.9 24.9 1.0 CG A:ASP136 2.9 28.0 1.0 OD2 A:ASP134 3.0 19.7 1.0 O A:ASN143 3.0 17.5 1.0 OD1 A:ASP134 3.1 17.0 1.0 CG A:ASP195 3.2 16.2 1.0 OD1 A:ASP136 3.4 30.2 1.0 C A:ASN104 3.4 23.1 1.0 CG A:ASP134 3.6 18.3 1.0 N A:ASN104 3.7 26.3 1.0 OD1 A:ASP195 3.8 17.1 1.0 CB A:ASN104 3.9 24.9 1.0 CA A:ASN104 3.9 24.4 1.0 CB A:ASP136 4.1 26.3 1.0 CB A:ASP195 4.2 15.2 1.0 C A:ASN143 4.2 19.6 1.0 CB A:ASN102 4.3 26.1 1.0 N A:ARG105 4.6 21.8 1.0 CD A:PRO106 4.6 14.4 1.0 CA A:ASN102 4.6 24.2 1.0 CG A:LEU201 4.6 27.3 1.0 CG A:PRO106 4.7 13.5 1.0 CB A:LEU201 4.7 25.7 1.0 N A:ASP103 4.7 25.3 1.0 C A:ASN102 4.7 23.8 1.0 CD1 A:LEU201 4.8 24.4 1.0 C A:ASP103 5.0 27.0 1.0

Calcium binding site 3 out of 3 in the E-Cadherin Activation


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of E-Cadherin Activation within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca703 b:30.9 occ:1.00 OD2 A:ASP67 2.6 20.4 1.0 CG A:ASP67 2.8 23.2 1.0 OE1 A:GLU69 2.8 30.4 1.0 OE1 A:GLU11 2.8 24.4 1.0 OD2 A:ASP103 2.9 31.1 1.0 OD1 A:ASP67 3.1 26.3 1.0 OD1 A:ASN12 3.6 34.6 1.0 CB A:ASP67 3.7 22.7 1.0 CA A:ASP67 3.8 22.4 1.0 CG A:ASP103 3.9 28.9 1.0 CD A:GLU69 4.0 25.0 1.0 OD1 A:ASP103 4.0 31.2 1.0 CD A:GLU11 4.1 25.7 1.0 ND2 A:ASN12 4.3 29.7 1.0 CG A:ASN12 4.3 31.2 1.0 N A:ARG68 4.3 21.4 1.0 C A:ASP67 4.4 21.3 1.0 CB A:GLU69 4.5 22.4 1.0 CG A:GLU69 4.6 24.0 1.0 CA A:CA701 4.6 19.5 1.0 O A:LEU66 4.6 20.3 1.0 N A:GLU69 4.6 21.9 1.0 OE2 A:GLU11 4.9 26.7 1.0 O A:HOH836 4.9 15.2 1.0 OE2 A:GLU69 4.9 17.9 1.0 N A:ASP67 4.9 22.6 1.0 CG A:GLU11 5.0 26.4 1.0

D.Haussinger, T.Ahrens, T.Aberle, J.Engel, J.Stetefeld, S.Grzesiek. Proteolytic E-Cadherin Activation Followed By Solution uc(Nmr) and X-Ray Crystallography. Embo J. V. 23 1699 2004.
ISSN: ISSN 0261-4189
PubMed: 15071499
DOI: 10.1038/SJ.EMBOJ.7600192