Magnesium in PDB 1p50: Transition State Structure of An Arginine Kinase Mutant

All present enzymatic activity of Transition State Structure of An Arginine Kinase Mutant:
2.7.3.3;

The structure of Transition State Structure of An Arginine Kinase Mutant, PDB code: 1p50 was solved by P.S.Pruett, A.Azzi, S.A.Clark, M.S.Yousef, J.L.Gattis, T.Somasundarum, W.R.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 / 2.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	65.454, 71.246, 80.116, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 24.6

The binding sites of Magnesium atom in the Transition State Structure of An Arginine Kinase Mutant (pdb code 1p50). 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 Transition State Structure of An Arginine Kinase Mutant, PDB code: 1p50:

Magnesium binding site 1 out of 1 in the Transition State Structure of An Arginine Kinase Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Transition State Structure of An Arginine Kinase Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:9.8 occ:1.00 O1 A:NO3401 2.0 21.1 1.0 O A:HOH473 2.1 37.7 1.0 O A:HOH421 2.1 34.1 1.0 O1A A:ADP400 2.2 18.6 1.0 O1B A:ADP400 2.5 18.4 1.0 N A:NO3401 3.3 21.5 1.0 PA A:ADP400 3.5 19.1 1.0 OE2 A:GLU314 3.6 19.9 1.0 PB A:ADP400 3.7 17.9 1.0 NE2 A:GLN225 3.8 20.1 1.0 O3 A:NO3401 3.8 21.2 1.0 NH2 A:ARG403 3.9 16.4 1.0 O A:HOH423 3.9 18.4 1.0 O3A A:ADP400 3.9 18.3 1.0 O A:HOH415 4.0 15.3 1.0 OE2 A:GLU224 4.2 20.0 1.0 NH1 A:ARG229 4.4 18.8 1.0 OE1 A:GLU224 4.4 18.9 1.0 CD A:GLU314 4.5 20.1 1.0 O2 A:NO3401 4.5 20.9 1.0 O3B A:ADP400 4.5 18.5 1.0 O2A A:ADP400 4.6 19.0 1.0 O5' A:ADP400 4.6 18.0 1.0 C5' A:ADP400 4.7 18.4 1.0 CD A:GLU224 4.7 18.8 1.0 CZ3 A:TRP221 4.8 18.7 1.0 O2B A:ADP400 4.8 19.0 1.0 CD A:GLN225 4.9 19.6 1.0 CG A:GLU314 4.9 20.5 1.0 NH1 A:ARG309 5.0 19.0 1.0

P.S.Pruett, A.Azzi, S.A.Clark, M.S.Yousef, J.L.Gattis, T.Somasundaram, W.R.Ellington, M.S.Chapman. The Putative Catalytic Bases Have, at Most, An Accessory Role in the Mechanism of Arginine Kinase. J.Biol.Chem. V. 278 26952 2003.
ISSN: ISSN 0021-9258
PubMed: 12732621
DOI: 10.1074/JBC.M212931200