Magnesium in PDB 4iir: Crystal Structure of Amppnp-Bound Human PRPF4B Kinase Domain

All present enzymatic activity of Crystal Structure of Amppnp-Bound Human PRPF4B Kinase Domain:
2.7.11.1;

The structure of Crystal Structure of Amppnp-Bound Human PRPF4B Kinase Domain, PDB code: 4iir was solved by I.Mechin, K.Haas, X.Chen, Y.Zhang, L.Mclean, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.16 / 2.00
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	52.500, 52.500, 78.790, 105.29, 103.05, 93.09
R / Rfree (%)	24.3 / 26.5

The binding sites of Magnesium atom in the Crystal Structure of Amppnp-Bound Human PRPF4B Kinase Domain (pdb code 4iir). 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 Amppnp-Bound Human PRPF4B Kinase Domain, PDB code: 4iir:

Magnesium binding site 1 out of 1 in the Crystal Structure of Amppnp-Bound Human PRPF4B Kinase Domain


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 Amppnp-Bound Human PRPF4B Kinase Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1103 b:75.2 occ:1.00 O1B A:ANP1101 2.0 80.2 1.0 O2G A:ANP1101 2.1 68.6 1.0 O A:HOH1331 2.6 61.0 1.0 O A:HOH1388 3.2 66.1 1.0 PG A:ANP1101 3.4 77.7 1.0 PB A:ANP1101 3.5 77.9 1.0 N3B A:ANP1101 4.0 60.5 1.0 C5' A:ANP1101 4.1 48.1 1.0 O2B A:ANP1101 4.3 74.0 1.0 O3G A:ANP1101 4.4 82.8 1.0 O3A A:ANP1101 4.4 56.3 1.0 O1G A:ANP1101 4.6 66.0 1.0 O1A A:ANP1101 4.6 50.7 1.0 O A:SER699 4.7 43.1 1.0 O A:GLN695 4.8 62.8 1.0

Q.Gao, I.Mechin, N.Kothari, Z.Guo, G.Deng, K.Haas, J.Mcmanus, D.Hoffmann, A.Wang, D.Wiederschain, J.Rocnik, W.Czechtizky, X.Chen, L.Mclean, H.Arlt, D.Harper, F.Liu, T.Majid, V.Patel, C.Lengauer, C.Garcia-Echeverria, B.Zhang, H.Cheng, M.Dorsch, S.M.Huang. Evaluation of Cancer Dependence and Druggability of PRP4 Kinase Using Cellular, Biochemical, and Structural Approaches. J.Biol.Chem. V. 288 30125 2013.
ISSN: ISSN 0021-9258
PubMed: 24003220
DOI: 10.1074/JBC.M113.473348