Magnesium in PDB 5zmf: Amppnp Complex of C. Reinhardtii ARSA1

The structure of Amppnp Complex of C. Reinhardtii ARSA1, PDB code: 5zmf was solved by T.W.Lin, C.D.Hsiao, H.Y.Chang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.72 / 3.56
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	90.456, 90.456, 306.668, 90.00, 90.00, 90.00
R / Rfree (%)	27.5 / 32.7

The binding sites of Magnesium atom in the Amppnp Complex of C. Reinhardtii ARSA1 (pdb code 5zmf). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Amppnp Complex of C. Reinhardtii ARSA1, PDB code: 5zmf:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Amppnp Complex of C. Reinhardtii ARSA1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Amppnp Complex of C. Reinhardtii ARSA1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg802 b:0.4 occ:1.00 OG1 A:THR116 2.6 0.6 1.0 O2G A:ANP801 3.0 0.9 1.0 OD2 A:ASP261 3.2 0.8 1.0 O1B A:ANP801 3.4 0.3 1.0 OD1 A:ASP261 3.5 0.4 1.0 CG A:ASP261 3.7 0.9 1.0 CB A:THR116 4.0 0.4 1.0 PG A:ANP801 4.1 0.1 1.0 OG A:SER143 4.1 0.8 1.0 CG A:LYS115 4.1 0.2 1.0 O2B A:ANP801 4.2 0.3 1.0 PB A:ANP801 4.2 0.6 1.0 N3B A:ANP801 4.3 0.2 1.0 O A:THR262 4.5 1.0 1.0 CD A:LYS115 4.5 0.4 1.0 O3G A:ANP801 4.5 0.3 1.0 CB A:SER143 4.6 0.0 1.0 OD2 A:ASP139 4.6 0.9 1.0 N A:THR116 4.7 0.4 1.0 CA A:THR116 4.7 0.5 1.0 CG2 A:THR116 4.8 0.7 1.0

Magnesium binding site 2 out of 2 in the Amppnp Complex of C. Reinhardtii ARSA1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Amppnp Complex of C. Reinhardtii ARSA1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg804 b:0.4 occ:1.00 OG1 A:THR460 2.5 0.2 1.0 O1G A:ANP803 3.4 0.8 1.0 OD1 A:ASP599 3.4 0.7 1.0 N A:THR460 3.7 0.6 1.0 CB A:THR460 3.7 0.2 1.0 OD2 A:ASP483 3.7 0.0 1.0 CG A:LYS459 3.7 0.0 1.0 O3A A:ANP803 3.8 0.1 1.0 O2A A:ANP803 3.9 0.4 1.0 CE A:LYS459 3.9 0.1 1.0 OD2 A:ASP599 4.0 0.9 1.0 CA A:THR460 4.1 0.3 1.0 CG A:ASP599 4.1 0.3 1.0 PA A:ANP803 4.2 0.6 1.0 NZ A:LYS459 4.3 0.3 1.0 C A:LYS459 4.3 0.3 1.0 CD A:LYS459 4.3 0.2 1.0 O1A A:ANP803 4.4 1.0 1.0 O A:THR600 4.4 0.9 1.0 CG A:PRO602 4.4 0.1 1.0 CG A:ASP483 4.6 0.2 1.0 O2B A:ANP803 4.6 0.3 1.0 OG A:SER487 4.6 0.4 1.0 N A:LYS459 4.6 0.1 1.0 CB A:SER487 4.7 0.7 1.0 CD A:PRO602 4.7 0.7 1.0 PB A:ANP803 4.7 0.6 1.0 PG A:ANP803 4.7 0.1 1.0 CA A:LYS459 4.8 0.6 1.0 CB A:ASP483 4.8 0.8 1.0 CB A:LYS459 4.8 0.8 1.0 CG2 A:THR460 4.9 0.3 1.0 O A:LYS459 4.9 0.6 1.0

T.W.Lin, C.C.Chen, S.M.Wu, Y.C.Chang, Y.C.Li, Y.W.Su, C.D.Hsiao, H.Y.Chang. Structural Analysis of Chloroplast Tail-Anchored Membrane Protein Recognition By ARSA1. Plant J. V. 99 128 2019.
ISSN: ESSN 1365-313X
PubMed: 30891827
DOI: 10.1111/TPJ.14316