Calcium in PDB 1vrk: The 1.9 Angstrom Structure of E84K-Calmodulin RS20 Peptide Complex

All present enzymatic activity of The 1.9 Angstrom Structure of E84K-Calmodulin RS20 Peptide Complex:
2.7.1.117;

The structure of The 1.9 Angstrom Structure of E84K-Calmodulin RS20 Peptide Complex, PDB code: 1vrk was solved by S.Weigand, W.F.Anderson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	61.209, 40.560, 32.774, 90.00, 91.70, 90.00
R / Rfree (%)	17.1 / 24.2

The binding sites of Calcium atom in the The 1.9 Angstrom Structure of E84K-Calmodulin RS20 Peptide Complex (pdb code 1vrk). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the The 1.9 Angstrom Structure of E84K-Calmodulin RS20 Peptide Complex, PDB code: 1vrk:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the The 1.9 Angstrom Structure of E84K-Calmodulin RS20 Peptide Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The 1.9 Angstrom Structure of E84K-Calmodulin RS20 Peptide Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca151 b:12.0 occ:1.00 O A:THR26 2.3 9.7 1.0 O A:HOH201 2.3 4.6 0.7 OD1 A:ASP20 2.4 9.8 1.0 OD1 A:ASP22 2.5 15.2 1.0 OE2 A:GLU31 2.5 16.3 1.0 OE1 A:GLU31 2.5 6.8 1.0 OD1 A:ASP24 2.6 12.5 1.0 CD A:GLU31 2.8 10.2 1.0 CG A:ASP24 3.3 16.9 1.0 CG A:ASP22 3.4 7.8 1.0 CG A:ASP20 3.5 9.6 1.0 C A:THR26 3.5 12.1 1.0 OD2 A:ASP24 3.7 16.5 1.0 OD2 A:ASP22 3.7 18.3 1.0 OG1 A:THR26 4.1 23.6 1.0 CA A:ASP20 4.1 8.8 1.0 N A:THR26 4.2 8.1 1.0 OD2 A:ASP20 4.3 12.8 1.0 CB A:ASP20 4.3 11.2 1.0 N A:ASP24 4.3 13.8 1.0 CG A:GLU31 4.3 2.0 1.0 CA A:THR26 4.4 13.6 1.0 N A:ILE27 4.5 8.5 1.0 N A:ASP22 4.5 22.9 1.0 CB A:ASP24 4.5 13.8 1.0 C A:ASP20 4.5 12.9 1.0 CA A:ILE27 4.5 8.8 1.0 N A:LYS21 4.6 19.3 1.0 N A:GLY23 4.7 17.8 1.0 O A:HOH209 4.7 2.2 0.5 CB A:ASP22 4.7 17.2 1.0 CA A:ASP24 4.8 12.7 1.0 N A:GLY25 4.9 7.1 1.0 O A:HOH505 4.9 19.4 0.5 CB A:THR26 4.9 21.7 1.0 N A:THR28 4.9 8.2 1.0 CA A:ASP22 5.0 19.5 1.0

Calcium binding site 2 out of 4 in the The 1.9 Angstrom Structure of E84K-Calmodulin RS20 Peptide Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The 1.9 Angstrom Structure of E84K-Calmodulin RS20 Peptide Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca152 b:7.6 occ:1.00 OD1 A:ASP56 2.4 6.1 1.0 OD1 A:ASP58 2.4 11.5 1.0 O A:THR62 2.4 6.5 1.0 OD1 A:ASN60 2.4 14.9 1.0 O A:HOH202 2.5 13.3 1.0 OE1 A:GLU67 2.6 11.1 1.0 OE2 A:GLU67 2.6 14.8 1.0 CD A:GLU67 2.9 14.9 1.0 CG A:ASN60 3.3 12.7 1.0 CG A:ASP58 3.4 9.6 1.0 CG A:ASP56 3.6 10.9 1.0 C A:THR62 3.6 8.7 1.0 OD2 A:ASP58 3.7 15.4 1.0 ND2 A:ASN60 3.8 11.3 1.0 CA A:ASP56 4.3 4.4 1.0 N A:ASN60 4.3 12.7 1.0 N A:THR62 4.3 8.1 1.0 O A:HOH504 4.3 49.1 1.0 OD2 A:ASP56 4.4 9.6 1.0 CG A:GLU67 4.4 11.8 1.0 CA A:ILE63 4.4 8.0 1.0 N A:ASP58 4.5 12.3 1.0 N A:ILE63 4.5 6.9 1.0 N A:ASP64 4.5 4.9 1.0 CB A:ASP56 4.5 2.0 1.0 CB A:ASN60 4.5 12.9 1.0 CA A:THR62 4.5 8.7 1.0 OG1 A:THR62 4.5 7.1 1.0 C A:ASP56 4.6 5.7 1.0 CB A:ASP58 4.6 6.3 1.0 O A:HOH506 4.7 19.5 1.0 CG A:ASP64 4.7 24.2 1.0 OD1 A:ASP64 4.8 30.7 1.0 CA A:ASN60 4.8 14.0 1.0 N A:GLY59 4.8 10.9 1.0 N A:ALA57 4.8 8.8 1.0 OD2 A:ASP64 4.8 30.8 1.0 C A:ILE63 4.9 6.2 1.0 CA A:ASP58 4.9 13.7 1.0 N A:GLY61 5.0 9.6 1.0

Calcium binding site 3 out of 4 in the The 1.9 Angstrom Structure of E84K-Calmodulin RS20 Peptide Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of The 1.9 Angstrom Structure of E84K-Calmodulin RS20 Peptide Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca153 b:36.6 occ:1.00 O A:PHE99 2.4 20.5 1.0 OD1 A:ASN97 2.4 43.6 1.0 OD1 A:ASP95 2.5 33.7 1.0 OE1 A:GLU104 2.6 31.7 1.0 O A:HOH203 2.7 18.9 0.6 OD1 A:ASP93 2.7 32.1 1.0 OE2 A:GLU104 2.7 33.3 1.0 CD A:GLU104 2.9 35.3 1.0 CG A:ASP95 3.3 40.0 1.0 OD2 A:ASP95 3.5 39.5 1.0 C A:PHE99 3.5 28.4 1.0 CG A:ASN97 3.6 44.7 1.0 CG A:ASP93 3.8 35.7 1.0 N A:ASN97 4.2 43.5 1.0 N A:PHE99 4.2 19.5 1.0 CA A:PHE99 4.3 26.8 1.0 CG A:GLU104 4.4 29.9 1.0 N A:ILE100 4.4 22.8 1.0 CA A:ASP93 4.4 27.0 1.0 CB A:ASN97 4.4 45.0 1.0 ND2 A:ASN97 4.5 41.8 1.0 CA A:ILE100 4.5 25.2 1.0 N A:ASP95 4.5 48.1 1.0 N A:GLY96 4.6 44.5 1.0 CB A:ASP95 4.6 37.5 1.0 CB A:PHE99 4.6 34.9 1.0 OD2 A:ASP93 4.7 30.7 1.0 C A:ASP93 4.7 29.5 1.0 CB A:ASP93 4.7 24.4 1.0 N A:SER101 4.7 21.4 1.0 CA A:ASN97 4.8 43.6 1.0 N A:LYS94 4.8 35.8 1.0 OG A:SER101 4.8 33.2 1.0 OE1 A:GLN135 4.8 63.5 1.0 CA A:ASP95 4.9 43.1 1.0 C A:ASP95 4.9 47.2 1.0

Calcium binding site 4 out of 4 in the The 1.9 Angstrom Structure of E84K-Calmodulin RS20 Peptide Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of The 1.9 Angstrom Structure of E84K-Calmodulin RS20 Peptide Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca154 b:33.3 occ:1.00 O A:GLN135 2.5 30.4 1.0 OD1 A:ASP129 2.5 22.2 1.0 OD1 A:ASP133 2.6 42.6 1.0 O A:HOH204 2.6 32.9 1.0 OE1 A:GLU140 2.6 33.2 1.0 OD1 A:ASP131 2.6 45.7 1.0 OE2 A:GLU140 2.7 40.5 1.0 CD A:GLU140 3.0 38.8 1.0 CG A:ASP131 3.4 43.4 1.0 C A:GLN135 3.5 29.5 1.0 CG A:ASP133 3.5 46.2 1.0 OD2 A:ASP131 3.6 41.9 1.0 CG A:ASP129 3.7 40.7 1.0 OD2 A:ASP133 4.0 36.4 1.0 CA A:ASP129 4.1 44.7 1.0 CA A:VAL136 4.1 27.8 1.0 N A:VAL136 4.2 32.4 1.0 N A:ASP133 4.2 44.5 1.0 CB A:ASP129 4.4 42.8 1.0 N A:GLN135 4.4 38.8 1.0 N A:ASN137 4.4 23.9 1.0 N A:ASP131 4.4 40.3 1.0 N A:VAL130 4.4 46.0 1.0 CG A:GLU140 4.5 34.2 1.0 CA A:GLN135 4.5 32.7 1.0 C A:ASP129 4.5 46.4 1.0 N A:GLY132 4.6 41.8 1.0 CB A:ASP133 4.6 40.5 1.0 CB A:ASP131 4.7 43.3 1.0 OD2 A:ASP129 4.7 32.8 1.0 C A:VAL136 4.7 16.4 1.0 CA A:ASP133 4.8 37.5 1.0 CA A:ASP131 4.9 42.6 1.0 OD1 A:ASN137 4.9 41.2 1.0 C A:ASP131 5.0 45.5 1.0 CG A:ASN137 5.0 30.4 1.0

S.Mirzoeva, S.Weigand, T.J.Lukas, L.Shuvalova, W.F.Anderson, D.M.Watterson. Analysis of the Functional Coupling Between Calmodulin'S Calcium Binding and Peptide Recognition Properties. Biochemistry V. 38 3936 1999.
ISSN: ISSN 0006-2960
PubMed: 10194305
DOI: 10.1021/BI9821263