Magnesium in PDB 3drb: Crystal Structure of Human Brain-Type Creatine Kinase

All present enzymatic activity of Crystal Structure of Human Brain-Type Creatine Kinase:
2.7.3.2;

The structure of Crystal Structure of Human Brain-Type Creatine Kinase, PDB code: 3drb was solved by J.H.Moon, S.M.Bong, K.Y.Hwang, Y.M.Chi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.17 / 2.00
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	97.720, 97.720, 166.910, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 22.7

The binding sites of Magnesium atom in the Crystal Structure of Human Brain-Type Creatine Kinase (pdb code 3drb). 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 Human Brain-Type Creatine Kinase, PDB code: 3drb:

Magnesium binding site 1 out of 1 in the Crystal Structure of Human Brain-Type Creatine Kinase


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 Human Brain-Type Creatine Kinase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg500 b:50.2 occ:1.00 O1B B:ADP400 2.4 51.2 1.0 O B:HOH851 2.6 36.0 1.0 O B:HOH953 2.6 38.2 1.0 O1A B:ADP400 3.1 37.9 1.0 O B:HOH1130 3.4 34.8 1.0 O3A B:ADP400 3.4 42.6 1.0 PB B:ADP400 3.5 40.1 1.0 PA B:ADP400 3.7 35.4 1.0 CZ3 B:TRP228 3.7 25.7 1.0 O B:HOH786 4.0 28.3 1.0 O B:HOH928 4.1 37.6 1.0 NH1 B:ARG236 4.1 24.5 1.0 O2B B:ADP400 4.2 54.9 1.0 O5' B:ADP400 4.2 39.6 1.0 CH2 B:TRP228 4.2 22.1 1.0 OE2 B:GLU231 4.3 24.4 1.0 O B:HOH875 4.3 39.7 1.0 OE1 B:GLU231 4.3 30.0 1.0 O B:HOH721 4.4 25.5 1.0 OE2 B:GLU232 4.7 31.1 1.0 CD B:GLU231 4.7 26.1 1.0 O B:HOH818 4.7 37.2 1.0 CE3 B:TRP228 4.9 23.8 1.0 O3B B:ADP400 5.0 46.2 1.0

S.M.Bong, J.H.Moon, K.H.Nam, K.S.Lee, Y.M.Chi, K.Y.Hwang. Structural Studies of Human Brain-Type Creatine Kinase Complexed with the Adp-MG2+-NO3- -Creatine Transition-State Analogue Complex Febs Lett. V. 582 3959 2008.
ISSN: ISSN 0014-5793
PubMed: 18977227
DOI: 10.1016/J.FEBSLET.2008.10.039