Magnesium in PDB 3lmg: Crystal Structure of the ERBB3 Kinase Domain in Complex with Amp-Pnp

All present enzymatic activity of Crystal Structure of the ERBB3 Kinase Domain in Complex with Amp-Pnp:
2.7.10.1;

The structure of Crystal Structure of the ERBB3 Kinase Domain in Complex with Amp-Pnp, PDB code: 3lmg was solved by F.Shi, M.A.Lemmon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	193.348, 47.981, 82.224, 90.00, 108.11, 90.00
R / Rfree (%)	25.2 / 28.5

The binding sites of Magnesium atom in the Crystal Structure of the ERBB3 Kinase Domain in Complex with Amp-Pnp (pdb code 3lmg). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the ERBB3 Kinase Domain in Complex with Amp-Pnp, PDB code: 3lmg:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the ERBB3 Kinase Domain in Complex with Amp-Pnp


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 the ERBB3 Kinase Domain in Complex with Amp-Pnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg202 b:49.8 occ:1.00 O2B A:ANP301 1.8 47.9 1.0 O2A A:ANP301 2.0 46.2 1.0 O1G A:ANP301 2.1 47.3 1.0 OD2 A:ASP833 2.1 32.5 1.0 OD1 A:ASN820 2.6 33.0 1.0 PB A:ANP301 3.0 47.8 1.0 PA A:ANP301 3.2 46.4 1.0 PG A:ANP301 3.3 48.0 1.0 CG A:ASP833 3.3 32.0 1.0 O3A A:ANP301 3.5 47.1 1.0 N3B A:ANP301 3.6 47.9 1.0 CG A:ASN820 3.8 33.5 1.0 O5' A:ANP301 3.8 46.0 1.0 O3G A:ANP301 4.0 48.1 1.0 NZ A:LYS723 4.2 30.2 1.0 CB A:ASP833 4.2 31.6 1.0 OD1 A:ASP833 4.2 32.3 1.0 O1B A:ANP301 4.4 48.0 1.0 O2G A:ANP301 4.5 47.9 1.0 O1A A:ANP301 4.5 46.4 1.0 O A:ARG819 4.5 33.6 1.0 ND2 A:ASN820 4.6 33.7 1.0 CA A:ASN820 4.7 33.5 1.0 CB A:ASN820 4.8 33.5 1.0 C A:ARG819 4.9 33.6 1.0 C2' A:ANP301 5.0 45.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the ERBB3 Kinase Domain in Complex with Amp-Pnp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the ERBB3 Kinase Domain in Complex with Amp-Pnp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg202 b:57.5 occ:1.00 O2B B:ANP301 1.9 38.4 1.0 OD2 B:ASP833 2.0 27.5 1.0 O2A B:ANP301 2.2 39.0 1.0 OD1 B:ASN820 2.4 23.9 1.0 O1G B:ANP301 2.5 38.2 1.0 PB B:ANP301 3.2 39.0 1.0 CG B:ASP833 3.2 27.2 1.0 PA B:ANP301 3.3 38.7 1.0 CG B:ASN820 3.6 23.9 1.0 O3A B:ANP301 3.6 39.3 1.0 O5' B:ANP301 3.7 38.7 1.0 PG B:ANP301 3.7 39.3 1.0 N3B B:ANP301 4.0 38.8 1.0 OD1 B:ASP833 4.0 28.1 1.0 O B:ARG819 4.2 23.4 1.0 CB B:ASP833 4.2 26.6 1.0 ND2 B:ASN820 4.3 24.0 1.0 NZ B:LYS723 4.3 28.8 1.0 O3G B:ANP301 4.4 39.7 1.0 O1B B:ANP301 4.4 39.1 1.0 O1A B:ANP301 4.7 39.0 1.0 CB B:ASN820 4.7 23.9 1.0 CA B:ASN820 4.7 23.9 1.0 C8 B:ANP301 4.7 38.9 1.0 C2' B:ANP301 4.8 40.1 1.0 C B:ARG819 4.9 23.4 1.0 C5' B:ANP301 4.9 39.4 1.0 O2G B:ANP301 4.9 39.3 1.0

F.Shi, S.E.Telesco, Y.Liu, R.Radhakrishnan, M.A.Lemmon. ERBB3/HER3 Intracellular Domain Is Competent to Bind Atp and Catalyze Autophosphorylation. Proc.Natl.Acad.Sci.Usa V. 107 7692 2010.
ISSN: ISSN 0027-8424
PubMed: 20351256
DOI: 10.1073/PNAS.1002753107