Calcium in PDB 5ar2: RIP2 Kinase Catalytic Domain (1 - 310)

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

The structure of RIP2 Kinase Catalytic Domain (1 - 310), PDB code: 5ar2 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)	20.00 / 2.44
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	132.566, 132.566, 107.788, 90.00, 90.00, 120.00
R / Rfree (%)	16.983 / 21.125

The binding sites of Calcium atom in the RIP2 Kinase Catalytic Domain (1 - 310) (pdb code 5ar2). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the RIP2 Kinase Catalytic Domain (1 - 310), PDB code: 5ar2:

Calcium binding site 1 out of 1 in the RIP2 Kinase Catalytic Domain (1 - 310)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of RIP2 Kinase Catalytic Domain (1 - 310) within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1311 b:58.2 occ:1.00 O B:HOH2080 2.4 64.7 1.0 O B:HOH2164 2.4 46.0 1.0 O B:HOH2078 2.4 45.0 1.0 O B:GLU112 2.5 46.1 1.0 O B:HOH2079 2.5 59.8 1.0 O B:HOH2165 2.6 55.8 1.0 O B:HOH2166 2.6 61.2 1.0 C B:GLU112 3.7 45.6 1.0 O B:HOH2034 4.0 54.2 1.0 O B:LEU309 4.3 32.8 1.0 OE2 B:GLU112 4.4 76.2 1.0 CD B:PRO114 4.4 41.2 1.0 CD B:GLU112 4.5 79.2 1.0 CA B:GLU112 4.5 45.3 1.0 N B:TYR113 4.7 37.0 1.0 O B:GLN308 4.7 32.5 1.0 OE1 B:GLU112 4.7 81.6 1.0 CA B:TYR113 4.7 38.4 1.0 O B:LYS310 4.8 43.1 1.0 CD1 B:TYR113 4.9 35.5 1.0 CG B:GLU112 4.9 61.4 1.0 O B:THR111 5.0 46.4 1.0 C B:LEU309 5.0 34.2 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