Magnesium in PDB 5v60: Phospho-ERK2 Bound to Amp-Pcp

All present enzymatic activity of Phospho-ERK2 Bound to Amp-Pcp:
2.7.11.24;

The structure of Phospho-ERK2 Bound to Amp-Pcp, PDB code: 5v60 was solved by B.C.Lechtenberg, S.J.Riedl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.60 / 2.18
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.757, 78.516, 152.566, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 22.6

The binding sites of Magnesium atom in the Phospho-ERK2 Bound to Amp-Pcp (pdb code 5v60). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Phospho-ERK2 Bound to Amp-Pcp, PDB code: 5v60:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Phospho-ERK2 Bound to Amp-Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Phospho-ERK2 Bound to Amp-Pcp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg408 b:45.0 occ:1.00 OD2 A:ASP167 2.2 43.3 1.0 O A:HOH550 2.2 52.3 1.0 O A:HOH501 2.2 47.8 1.0 O2A A:ACP401 2.2 45.6 1.0 OD1 A:ASN154 2.2 42.2 1.0 O2G A:ACP401 2.2 60.9 1.0 CG A:ASP167 3.2 40.3 1.0 CG A:ASN154 3.2 38.3 1.0 PG A:ACP401 3.5 58.1 1.0 C3B A:ACP401 3.5 54.5 1.0 ND2 A:ASN154 3.6 35.7 1.0 PA A:ACP401 3.6 43.0 1.0 CB A:ASP167 3.7 38.5 1.0 MG A:MG409 3.8 49.0 1.0 O2B A:ACP401 4.1 48.3 1.0 OD1 A:ASP167 4.2 43.4 1.0 PB A:ACP401 4.2 49.9 1.0 O3G A:ACP401 4.3 57.6 1.0 O3A A:ACP401 4.3 45.9 1.0 OG A:SER153 4.3 42.4 1.0 CE A:LYS151 4.4 39.4 1.0 OD2 A:ASP149 4.5 46.5 1.0 O3' A:ACP401 4.6 44.7 1.0 O5' A:ACP401 4.6 45.3 1.0 O1A A:ACP401 4.6 45.0 1.0 CB A:ASN154 4.6 36.9 1.0 O1G A:ACP401 4.6 58.0 1.0 C5' A:ACP401 4.7 44.3 1.0 NZ A:LYS151 4.7 40.2 1.0 O A:HOH552 4.8 53.0 1.0 O A:SER153 4.8 42.0 1.0 C3' A:ACP401 5.0 43.5 1.0 CA A:ASN154 5.0 37.0 1.0

Magnesium binding site 2 out of 2 in the Phospho-ERK2 Bound to Amp-Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Phospho-ERK2 Bound to Amp-Pcp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg409 b:49.0 occ:1.00 O2B A:ACP401 2.2 48.3 1.0 O A:HOH508 2.2 51.0 1.0 O A:HOH552 2.2 53.0 1.0 O2G A:ACP401 2.2 60.9 1.0 O1G A:ACP401 2.2 58.0 1.0 OD1 A:ASP167 2.2 43.4 1.0 OD2 A:ASP167 2.4 43.3 1.0 CG A:ASP167 2.6 40.3 1.0 PG A:ACP401 2.8 58.1 1.0 PB A:ACP401 3.4 49.9 1.0 C3B A:ACP401 3.7 54.5 1.0 MG A:MG408 3.8 45.0 1.0 O A:HOH501 4.0 47.8 1.0 O3G A:ACP401 4.1 57.6 1.0 CB A:ASP167 4.2 38.5 1.0 O2A A:ACP401 4.3 45.6 1.0 O1B A:ACP401 4.4 49.8 1.0 OD2 A:ASP149 4.4 46.5 1.0 O3A A:ACP401 4.5 45.9 1.0 CA A:GLY169 4.6 39.1 1.0 NZ A:LYS54 4.6 48.2 1.0 PA A:ACP401 4.7 43.0 1.0 N A:GLY169 4.7 38.2 1.0 NH2 A:ARG67 4.9 56.3 1.0 CA A:ASP167 4.9 37.1 1.0

B.C.Lechtenberg, P.D.Mace, E.H.Sessions, R.Williamson, R.Stalder, Y.Wallez, G.P.Roth, S.J.Riedl, E.B.Pasquale. Structure-Guided Strategy For the Development of Potent Bivalent Erk Inhibitors. Acs Med Chem Lett V. 8 726 2017.
ISSN: ISSN 1948-5875
PubMed: 28740606
DOI: 10.1021/ACSMEDCHEMLETT.7B00127