Chlorine in PDB 2vay: Calmodulin Complexed with CAV1.1 Iq Peptide

The structure of Calmodulin Complexed with CAV1.1 Iq Peptide, PDB code: 2vay was solved by D.B.Halling, D.J.Black, S.E.Pedersen, S.L.Hamilton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.77 / 1.94
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	84.920, 34.670, 62.980, 90.00, 113.69, 90.00
R / Rfree (%)	21.8 / 27.2

The structure of Calmodulin Complexed with CAV1.1 Iq Peptide also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Chlorine atom in the Calmodulin Complexed with CAV1.1 Iq Peptide (pdb code 2vay). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Calmodulin Complexed with CAV1.1 Iq Peptide, PDB code: 2vay:

Chlorine binding site 1 out of 1 in the Calmodulin Complexed with CAV1.1 Iq Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Calmodulin Complexed with CAV1.1 Iq Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl2543 b:30.8 occ:1.00 NZ A:LYS75 2.6 28.8 1.0 O A:HOH2072 3.0 35.6 1.0 O B:HOH2001 3.1 49.9 1.0 O A:HOH2078 3.1 25.4 1.0 N B:TYR1524 3.4 20.0 1.0 CE A:MET71 3.5 26.6 1.0 N B:PHE1523 3.5 23.0 1.0 CB B:PHE1523 3.7 21.5 1.0 CE A:LYS75 3.8 27.0 1.0 CB B:TYR1524 3.9 21.4 1.0 CA B:PHE1523 4.0 21.6 1.0 O A:HOH2056 4.1 46.0 1.0 SD A:MET71 4.1 25.1 1.0 C B:PHE1523 4.2 21.8 1.0 CD1 B:PHE1523 4.2 20.8 1.0 N B:LYS1522 4.2 30.5 1.0 O A:HOH2079 4.2 43.9 1.0 O A:HOH2053 4.3 28.5 1.0 CA B:TYR1524 4.3 18.5 1.0 C B:LYS1522 4.3 26.6 1.0 CD A:LYS75 4.3 26.9 1.0 CG B:PHE1523 4.5 18.5 1.0 CA B:LYS1522 4.5 28.7 1.0 OE1 A:GLU84 4.6 34.6 1.0 O B:HOH2002 4.7 33.5 1.0 OE2 A:GLU84 5.0 34.9 1.0 N B:ALA1525 5.0 18.3 1.0

D.B.Halling, D.K.Georgiou, D.J.Black, G.Yang, J.L.Fallon, F.A.Quiocho, S.E.Pedersen, S.L.Hamilton. Determinants in CAV1 Channels That Regulate the CA2+ Sensitivity of Bound Calmodulin. J.Biol.Chem. V. 284 20041 2009.
ISSN: ISSN 0021-9258
PubMed: 19473981
DOI: 10.1074/JBC.M109.013326