Calcium in PDB 2nce: Solution Structure of CA2+-Bound C2 Domain From Protein Kinase C Alpha in the Form of Complex with V5-Phm Peptide

All present enzymatic activity of Solution Structure of CA2+-Bound C2 Domain From Protein Kinase C Alpha in the Form of Complex with V5-Phm Peptide:
2.7.11.13;

The binding sites of Calcium atom in the Solution Structure of CA2+-Bound C2 Domain From Protein Kinase C Alpha in the Form of Complex with V5-Phm Peptide (pdb code 2nce). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Solution Structure of CA2+-Bound C2 Domain From Protein Kinase C Alpha in the Form of Complex with V5-Phm Peptide, PDB code: 2nce:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Solution Structure of CA2+-Bound C2 Domain From Protein Kinase C Alpha in the Form of Complex with V5-Phm Peptide


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Solution Structure of CA2+-Bound C2 Domain From Protein Kinase C Alpha in the Form of Complex with V5-Phm Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:0.5 occ:1.00 OD2 A:ASP193 1.9 0.9 1.0 OD1 A:ASP246 1.9 0.5 1.0 OD2 A:ASP187 1.9 0.7 1.0 OD1 A:ASP248 2.0 0.6 1.0 OD1 A:ASP193 2.1 0.7 1.0 CG A:ASP193 2.2 0.6 1.0 CG A:ASP187 2.5 0.5 1.0 O A:TRP247 2.5 0.6 1.0 OD1 A:ASP187 2.6 0.5 1.0 CG A:ASP246 2.9 0.5 1.0 CG A:ASP248 3.2 0.6 1.0 OD2 A:ASP246 3.3 0.6 1.0 C A:TRP247 3.4 0.5 1.0 CA A:CA302 3.6 0.5 1.0 HA A:ASP248 3.6 0.7 1.0 CB A:ASP193 3.7 0.5 1.0 H A:ASP193 3.8 0.5 1.0 OD2 A:ASP248 3.8 0.7 1.0 CB A:ASP187 4.0 0.4 1.0 H A:TRP247 4.0 0.5 1.0 N A:TRP247 4.0 0.5 1.0 N A:ASP248 4.1 0.6 1.0 HB2 A:ASP193 4.2 0.6 1.0 CA A:ASP248 4.2 0.7 1.0 O A:ASP193 4.2 0.4 1.0 CB A:ASP248 4.2 0.7 1.0 CB A:ASP246 4.3 0.5 1.0 HB2 A:ASP187 4.3 0.5 1.0 N A:ASP193 4.3 0.4 1.0 HB3 A:ASP193 4.3 0.5 1.0 CA A:TRP247 4.3 0.6 1.0 C A:ASP246 4.3 0.5 1.0 HB3 A:ASP187 4.4 0.5 1.0 CA A:ASP193 4.5 0.4 1.0 HB2 A:ASP246 4.6 0.6 1.0 C A:ASP193 4.7 0.4 1.0 HB3 A:TRP247 4.7 0.7 1.0 CA A:ASP246 4.8 0.5 1.0 HA A:SER192 4.8 0.5 1.0 HA A:ASP246 4.8 0.5 1.0 O A:ASP246 4.8 0.5 1.0 HA A:ASP187 4.9 0.4 1.0 HB2 A:ASP248 4.9 0.8 1.0 HB2 A:MET186 4.9 0.7 1.0 HB3 A:ASP248 4.9 0.8 1.0 H A:ASP248 5.0 0.7 1.0 CA A:ASP187 5.0 0.4 1.0

Calcium binding site 2 out of 2 in the Solution Structure of CA2+-Bound C2 Domain From Protein Kinase C Alpha in the Form of Complex with V5-Phm Peptide


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Solution Structure of CA2+-Bound C2 Domain From Protein Kinase C Alpha in the Form of Complex with V5-Phm Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca302 b:0.5 occ:1.00 OD2 A:ASP248 1.8 0.7 1.0 OD2 A:ASP246 1.8 0.6 1.0 OD2 A:ASP254 1.8 0.9 1.0 OD1 A:ASP187 1.9 0.5 1.0 CG A:ASP248 2.5 0.6 1.0 O A:MET186 2.6 0.5 1.0 OD1 A:ASP248 2.6 0.6 1.0 CG A:ASP246 2.9 0.5 1.0 CG A:ASP187 3.0 0.5 1.0 HB3 A:MET186 3.0 0.8 1.0 CG A:ASP254 3.0 0.7 1.0 C A:MET186 3.1 0.5 1.0 HA A:ASP187 3.1 0.4 1.0 HB2 A:ASP254 3.3 1.1 1.0 HB2 A:MET186 3.3 0.7 1.0 OD1 A:ASP246 3.4 0.5 1.0 CB A:MET186 3.6 0.6 1.0 N A:ASP187 3.6 0.4 1.0 CA A:CA301 3.6 0.5 1.0 CA A:ASP187 3.7 0.4 1.0 OD2 A:ASP187 3.7 0.7 1.0 CB A:ASP254 3.7 0.8 1.0 H A:ASP254 3.8 1.1 1.0 CB A:ASP248 3.9 0.7 1.0 CB A:ASP187 3.9 0.4 1.0 CA A:MET186 3.9 0.5 1.0 OD1 A:ASP254 4.0 1.1 1.0 HB2 A:ASP248 4.0 0.8 1.0 HB3 A:ASP246 4.1 0.5 1.0 CB A:ASP246 4.2 0.5 1.0 O A:ARG252 4.2 2.4 1.0 H A:ASP187 4.3 0.5 1.0 HB3 A:ASP248 4.3 0.8 1.0 HB3 A:ASP254 4.5 1.3 1.0 HA A:MET186 4.5 0.6 1.0 N A:ASP254 4.5 0.8 1.0 HB2 A:ASP187 4.6 0.5 1.0 OD1 A:ASP193 4.6 0.7 1.0 HB3 A:ASP187 4.7 0.5 1.0 HB2 A:ASP246 4.7 0.6 1.0 CA A:ASP254 4.7 0.7 1.0 HD2 A:PRO188 4.8 0.6 1.0 O A:ASP246 4.9 0.5 1.0 CG A:MET186 4.9 0.8 1.0 CA A:ASP248 4.9 0.7 1.0 HA A:ASN253 5.0 1.9 1.0 HA A:ASP248 5.0 0.7 1.0

Y.Yang, T.I.Igumenova. CA2+-Sensing Domain Contributes to Auto-Inhibition of Protein Kinase Calpha Through Interactions with C-Terminal Tail To Be Published.