Calcium in PDB 3gif: Crystal Structure of DESKC_H188E in Complex with Adp

All present enzymatic activity of Crystal Structure of DESKC_H188E in Complex with Adp:
2.7.13.3;

The structure of Crystal Structure of DESKC_H188E in Complex with Adp, PDB code: 3gif was solved by F.Trajtenberg, D.Albanesi, P.M.Alzari, A.Buschiazzo, D.De Mendoza, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.27 / 2.70
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	91.580, 93.480, 59.420, 90.00, 90.00, 90.00
R / Rfree (%)	25.4 / 31.7

The binding sites of Calcium atom in the Crystal Structure of DESKC_H188E in Complex with Adp (pdb code 3gif). 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 Crystal Structure of DESKC_H188E in Complex with Adp, PDB code: 3gif:

Calcium binding site 1 out of 1 in the Crystal Structure of DESKC_H188E in Complex with Adp


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of DESKC_H188E in Complex with Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1303 b:66.5 occ:1.00 O A:HOH20 2.3 53.0 1.0 O1A A:ADP1301 2.3 71.2 1.0 OE2 A:GLU289 2.3 66.1 1.0 O3B A:ADP1301 2.3 76.6 1.0 OD1 A:ASN293 2.3 66.6 1.0 CD A:GLU289 3.2 61.9 1.0 PA A:ADP1301 3.4 72.4 1.0 CG A:ASN293 3.4 65.3 1.0 PB A:ADP1301 3.4 73.4 1.0 OE1 A:GLU289 3.5 52.7 1.0 O3A A:ADP1301 3.5 77.1 1.0 ND2 A:ASN293 3.7 64.0 1.0 O1B A:ADP1301 3.8 75.0 1.0 CA A:GLY336 3.9 66.1 1.0 N A:GLY336 3.9 71.8 1.0 O5' A:ADP1301 4.3 71.9 1.0 O2A A:ADP1301 4.5 69.5 1.0 CG A:GLU289 4.6 51.3 1.0 O2B A:ADP1301 4.7 70.6 1.0 CB A:ASN293 4.8 62.6 1.0 NE2 A:HIS297 4.8 78.4 1.0 C A:GLY336 5.0 67.0 1.0

D.Albanesi, M.Martin, F.Trajtenberg, M.C.Mansilla, A.Haouz, P.M.Alzari, D.De Mendoza, A.Buschiazzo. Structural Plasticity and Catalysis Regulation of A Thermosensor Histidine Kinase Proc.Natl.Acad.Sci.Usa V. 106 16185 2009.
ISSN: ISSN 0027-8424
PubMed: 19805278
DOI: 10.1073/PNAS.0906699106