Magnesium in PDB 1rl9: Crystal Structure of Creatine-Adp Arginine Kinase Ternary Complex

All present enzymatic activity of Crystal Structure of Creatine-Adp Arginine Kinase Ternary Complex:
2.7.3.3;

The structure of Crystal Structure of Creatine-Adp Arginine Kinase Ternary Complex, PDB code: 1rl9 was solved by A.Azzi, S.A.Clark, R.W.Ellington, M.S.Chapman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.100, 65.300, 85.800, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 23.7

The binding sites of Magnesium atom in the Crystal Structure of Creatine-Adp Arginine Kinase Ternary Complex (pdb code 1rl9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Creatine-Adp Arginine Kinase Ternary Complex, PDB code: 1rl9:

Magnesium binding site 1 out of 1 in the Crystal Structure of Creatine-Adp Arginine Kinase Ternary Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Creatine-Adp Arginine Kinase Ternary Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg901 b:11.4 occ:1.00 O1B A:ADP900 2.1 11.4 1.0 O A:HOH576 2.1 12.9 1.0 O A:HOH429 2.1 10.3 1.0 O A:HOH570 2.1 11.6 1.0 O A:HOH573 2.1 13.8 1.0 O1A A:ADP900 2.1 10.3 1.0 PB A:ADP900 3.3 10.9 1.0 PA A:ADP900 3.3 9.8 1.0 O3A A:ADP900 3.6 11.1 1.0 O A:HOH584 3.8 14.9 1.0 OE2 A:GLU314 4.0 16.6 1.0 O3B A:ADP900 4.1 12.9 1.0 OE2 A:GLU224 4.1 12.2 1.0 NH1 A:ARG229 4.3 10.1 1.0 OE2 A:GLU225 4.3 13.7 1.0 O2B A:ADP900 4.3 16.1 1.0 CZ3 A:TRP221 4.3 11.0 1.0 O2A A:ADP900 4.3 9.9 1.0 O A:HOH583 4.3 19.1 1.0 OE1 A:GLU224 4.4 10.6 1.0 C5' A:ADP900 4.4 9.2 1.0 O5' A:ADP900 4.4 10.5 1.0 O A:HOH368 4.5 11.5 1.0 CH2 A:TRP221 4.6 9.7 1.0 CD A:GLU314 4.7 21.6 1.0 CD A:GLU224 4.7 12.3 1.0 CG A:GLU314 4.8 15.0 1.0 O A:HOH439 4.8 12.4 1.0 NH1 A:ARG309 4.9 10.9 1.0

A.Azzi, S.A.Clark, W.R.Ellington, M.S.Chapman. The Role of Phosphagen Specificity Loops in Arginine Kinase. Protein Sci. V. 13 575 2004.
ISSN: ISSN 0961-8368
PubMed: 14978299
DOI: 10.1110/PS.03428304