Magnesium in PDB 5ar3: RIP2 Kinase Catalytic Domain (1 - 310) Complex with Amp-Pcp

All present enzymatic activity of RIP2 Kinase Catalytic Domain (1 - 310) Complex with Amp-Pcp:
2.7.11.1;

The structure of RIP2 Kinase Catalytic Domain (1 - 310) Complex with Amp-Pcp, PDB code: 5ar3 was solved by A.K.Charnley, M.A.Convery, A.Lakdawala Shah, E.Jones, P.Hardwicke, A.Bridges, B.J.Votta, P.J.Gough, R.W.Marquis, J.Bertin, L.Casillas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 3.23
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	131.566, 131.566, 106.582, 90.00, 90.00, 120.00
R / Rfree (%)	19 / 25.4

The binding sites of Magnesium atom in the RIP2 Kinase Catalytic Domain (1 - 310) Complex with Amp-Pcp (pdb code 5ar3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the RIP2 Kinase Catalytic Domain (1 - 310) Complex with Amp-Pcp, PDB code: 5ar3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the RIP2 Kinase Catalytic Domain (1 - 310) Complex with Amp-Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of RIP2 Kinase Catalytic Domain (1 - 310) Complex with Amp-Pcp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1312 b:84.0 occ:1.00 O1A A:ACP1311 2.2 93.8 1.0 OD2 A:ASP164 2.2 72.4 1.0 O2B A:ACP1311 2.2 99.2 1.0 OD1 A:ASN151 2.2 78.8 1.0 O A:HOH2023 2.3 55.0 1.0 CG A:ASP164 3.1 66.4 1.0 PB A:ACP1311 3.2 1.0 1.0 CG A:ASN151 3.3 63.7 1.0 PA A:ACP1311 3.3 96.4 1.0 O1B A:ACP1311 3.4 0.1 1.0 CB A:ASP164 3.6 60.2 1.0 O A:HOH2022 3.6 70.2 1.0 O3A A:ACP1311 3.6 96.0 1.0 ND2 A:ASN151 3.7 63.7 1.0 C5' A:ACP1311 3.8 82.3 1.0 O5' A:ACP1311 4.1 93.5 1.0 OD1 A:ASP164 4.1 68.1 1.0 CE A:LYS148 4.4 76.3 1.0 CB A:ASN151 4.6 54.0 1.0 O2A A:ACP1311 4.7 86.3 1.0 C3B A:ACP1311 4.8 0.5 1.0 CA A:ASN151 4.8 51.2 1.0 NZ A:LYS148 4.9 72.5 1.0 O A:HOH2045 5.0 40.3 1.0 CA A:ASP164 5.0 55.2 1.0

Magnesium binding site 2 out of 2 in the RIP2 Kinase Catalytic Domain (1 - 310) Complex with Amp-Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of RIP2 Kinase Catalytic Domain (1 - 310) Complex with Amp-Pcp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1312 b:77.7 occ:1.00 OD1 B:ASN151 2.2 77.5 1.0 O2B B:ACP1311 2.2 91.9 1.0 OD2 B:ASP164 2.2 74.1 1.0 O1A B:ACP1311 2.2 83.5 1.0 CG B:ASP164 3.1 68.1 1.0 CG B:ASN151 3.2 73.1 1.0 PB B:ACP1311 3.3 0.1 1.0 PA B:ACP1311 3.4 79.7 1.0 CB B:ASP164 3.5 58.7 1.0 O3A B:ACP1311 3.7 86.5 1.0 ND2 B:ASN151 3.7 77.4 1.0 O1B B:ACP1311 3.8 95.0 1.0 C5' B:ACP1311 3.9 70.3 1.0 O B:HOH2022 4.0 40.0 1.0 O5' B:ACP1311 4.2 71.8 1.0 OD1 B:ASP164 4.2 69.2 1.0 CB B:ASN151 4.5 62.8 1.0 O B:GLN150 4.6 63.8 1.0 O2A B:ACP1311 4.7 77.5 1.0 CA B:ASN151 4.8 57.8 1.0 C3B B:ACP1311 4.8 0.9 1.0 CA B:ASP164 4.9 57.4 1.0 C B:GLN150 4.9 61.5 1.0

A.K.Charnley, M.A.Convery, A.Lakdawala Shah, E.Jones, P.Hardwicke, A.Bridges, M.Ouellette, R.Totoritis, B.Schwartz, B.W.King, D.D.Wisnoski, J.Kang, P.M.Eidam, B.J.Votta, P.J.Gough, R.W.Marquis, J.Bertin, L.Casillas. Crystal Structures of Human RIP2 Kinase Catalytic Domain Complexed with Atp-Competitive Inhibitors: Foundations For Understanding Inhibitor Selectivity. Bioorg.Med.Chem. V. 23 7000 2015.
ISSN: ISSN 0968-0896
PubMed: 26455654
DOI: 10.1016/J.BMC.2015.09.038