Magnesium in PDB 2p0c: Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer

All present enzymatic activity of Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer:
2.7.10.1;

The structure of Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer, PDB code: 2p0c was solved by J.R.Walker, X.Huang, P.J.Finerty Jr., J.Weigelt, M.Sundstrom, C.H.Arrowsmith, A.M.Edwards, A.Bochkarev, S.Dhe-Paganon, Structuralgenomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.79 / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.470, 90.057, 69.253, 90.00, 102.44, 90.00
R / Rfree (%)	20.4 / 27.4

The binding sites of Magnesium atom in the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer (pdb code 2p0c). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer, PDB code: 2p0c:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg4 b:51.4 occ:1.00 N3B A:ANP1 1.8 57.0 1.0 O1A A:ANP1 2.0 47.8 1.0 OD1 A:ASP741 2.0 51.5 1.0 OD1 A:ASN728 2.2 39.8 1.0 O2G A:ANP1 2.6 56.0 1.0 PG A:ANP1 2.9 61.0 1.0 PB A:ANP1 3.1 52.6 1.0 PA A:ANP1 3.2 46.7 1.0 CG A:ASP741 3.3 50.0 1.0 CG A:ASN728 3.4 41.5 1.0 O1B A:ANP1 3.5 53.2 1.0 O3A A:ANP1 3.5 50.0 1.0 O3G A:ANP1 3.8 59.8 1.0 O1G A:ANP1 3.9 60.1 1.0 O A:HOH121 4.0 74.8 1.0 OD2 A:ASP741 4.1 53.8 1.0 ND2 A:ASN728 4.1 39.9 1.0 CB A:ASP741 4.1 48.8 1.0 O A:ARG727 4.2 41.1 1.0 O5' A:ANP1 4.2 46.3 1.0 O2A A:ANP1 4.3 50.5 1.0 O2B A:ANP1 4.3 54.3 1.0 CB A:ASN728 4.4 40.1 1.0 CA A:ASN728 4.4 40.2 1.0 O A:HOH84 4.6 45.7 1.0 C A:ARG727 4.7 40.7 1.0 N A:ASN728 4.8 40.4 1.0 CE A:MET730 4.9 48.6 1.0

Magnesium binding site 2 out of 3 in the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg5 b:42.5 occ:1.00 OD2 B:ASP741 2.0 48.3 1.0 O3A B:ANP2 2.1 56.2 1.0 O B:HOH129 2.1 46.7 1.0 OD1 B:ASN728 2.2 39.9 1.0 O1A B:ANP2 2.3 50.5 1.0 PA B:ANP2 2.8 49.6 1.0 PB B:ANP2 3.2 54.1 1.0 O2B B:ANP2 3.2 58.2 1.0 CG B:ASP741 3.2 48.8 1.0 CG B:ASN728 3.4 37.8 1.0 O2A B:ANP2 3.9 51.7 1.0 O B:HOH163 4.0 51.1 1.0 ND2 B:ASN728 4.0 39.2 1.0 O5' B:ANP2 4.0 50.9 1.0 OD1 B:ASP741 4.0 51.7 1.0 N3B B:ANP2 4.1 61.1 1.0 O B:HOH158 4.2 63.5 1.0 CB B:ASP741 4.2 47.1 1.0 O1B B:ANP2 4.3 59.0 1.0 O B:ARG727 4.3 36.0 1.0 CB B:ASN728 4.5 35.8 1.0 O B:HOH170 4.6 30.1 1.0 CA B:ASN728 4.6 36.6 1.0 C B:ARG727 4.9 36.5 1.0 CG B:ARG727 4.9 40.1 1.0

Magnesium binding site 3 out of 3 in the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg6 b:67.8 occ:1.00 OE2 B:GLU712 2.8 42.9 1.0 ND2 B:ASN716 2.9 53.7 1.0 OD1 B:ASN716 3.3 54.8 1.0 CG B:ASN716 3.5 53.4 1.0 CD B:GLU712 3.6 42.2 1.0 CG B:GLU712 3.7 38.9 1.0 CB B:SER848 3.8 43.6 1.0 OG B:SER848 4.6 48.6 1.0 OE1 B:GLU712 4.7 40.4 1.0 CB B:ASN716 5.0 51.6 1.0

X.Huang, P.Finerty, J.R.Walker, C.Butler-Cole, M.Vedadi, M.Schapira, S.A.Parker, B.E.Turk, D.A.Thompson, S.Dhe-Paganon. Structural Insights Into the Inhibited States of the Mer Receptor Tyrosine Kinase. J.Struct.Biol. V. 165 88 2009.
ISSN: ISSN 1047-8477
PubMed: 19028587
DOI: 10.1016/J.JSB.2008.10.003