Calcium in PDB 4tyq: Crystal Structure of An Adenylate Kinase Mutant--AKM2

All present enzymatic activity of Crystal Structure of An Adenylate Kinase Mutant--AKM2:
2.7.4.3;

The structure of Crystal Structure of An Adenylate Kinase Mutant--AKM2, PDB code: 4tyq was solved by S.Moon, E.Bae, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.65
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	39.003, 48.790, 54.832, 90.98, 97.34, 95.83
R / Rfree (%)	17.5 / 21.9

The structure of Crystal Structure of An Adenylate Kinase Mutant--AKM2 also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Zinc	(Zn)	2 atoms

The binding sites of Calcium atom in the Crystal Structure of An Adenylate Kinase Mutant--AKM2 (pdb code 4tyq). 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 An Adenylate Kinase Mutant--AKM2, PDB code: 4tyq:

Calcium binding site 1 out of 1 in the Crystal Structure of An Adenylate Kinase Mutant--AKM2


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 An Adenylate Kinase Mutant--AKM2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca304 b:20.8 occ:1.00 O A:GLN198 2.4 11.6 1.0 O A:HOH502 2.4 21.2 1.0 O A:HOH439 2.4 24.1 1.0 O A:HOH483 2.4 25.1 1.0 O A:HOH557 2.5 27.0 1.0 C A:GLN198 3.4 13.2 1.0 CA A:GLN198 4.1 14.0 1.0 OE2 A:GLU119 4.3 15.6 1.0 O A:GLN199 4.3 12.6 1.0 C A:GLN199 4.4 10.6 1.0 N A:GLN199 4.4 12.1 1.0 O A:HOH530 4.5 35.9 1.0 CB A:GLN198 4.5 17.1 1.0 OE1 A:GLU119 4.6 16.4 1.0 CA A:GLN199 4.6 11.6 1.0 N1A A:AP5301 4.7 8.5 1.0 N A:ASP200 4.8 10.9 1.0 CD A:GLU119 4.9 16.4 1.0 CG A:GLN198 5.0 20.8 1.0

S.Moon, E.Bae. Crystal Structures of Thermally Stable Adenylate Kinase Mutants Designed By Local Structural Entropy Optimization and Structure-Guided Mutagenesis J Korean Soc Appl Biol Chem V. 57 661 2014.
ISSN: ISSN 1738-2203
DOI: 10.1007/S13765-014-4228-4