Magnesium in PDB 6i7i: Crystal Structure of Dimeric Ficd Mutant K256A Complexed with Mgatp

The structure of Crystal Structure of Dimeric Ficd Mutant K256A Complexed with Mgatp, PDB code: 6i7i was solved by L.A.Perera, Y.Yan, R.J.Read, D.Ron, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	67.11 / 2.33
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.902, 73.983, 134.039, 90.00, 90.00, 90.00
R / Rfree (%)	28.3 / 32.5

The binding sites of Magnesium atom in the Crystal Structure of Dimeric Ficd Mutant K256A Complexed with Mgatp (pdb code 6i7i). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Dimeric Ficd Mutant K256A Complexed with Mgatp, PDB code: 6i7i:

Magnesium binding site 1 out of 1 in the Crystal Structure of Dimeric Ficd Mutant K256A Complexed with Mgatp


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 Dimeric Ficd Mutant K256A Complexed with Mgatp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:45.1 occ:1.00 O A:HOH614 1.9 59.6 1.0 O2B A:ATP502 2.1 46.4 1.0 O2A A:ATP502 2.1 44.5 1.0 OD1 A:ASP367 2.1 42.4 1.0 O A:HOH652 2.2 52.5 1.0 O A:HOH619 2.4 31.4 1.0 PB A:ATP502 3.1 46.4 1.0 CG A:ASP367 3.1 41.0 1.0 O3B A:ATP502 3.2 48.4 1.0 PA A:ATP502 3.4 44.0 1.0 OD2 A:ASP367 3.5 41.1 1.0 O3A A:ATP502 3.7 45.5 1.0 O A:HOH629 3.9 57.3 1.0 O1A A:ATP502 4.3 43.7 1.0 NH2 A:ARG371 4.4 39.8 1.0 N A:GLY368 4.4 38.4 1.0 CB A:ASP367 4.5 40.4 1.0 O5' A:ATP502 4.5 44.3 1.0 O1B A:ATP502 4.5 46.2 1.0 PG A:ATP502 4.7 50.0 0.5 C5' A:ATP502 4.8 44.0 1.0 CA A:ASP367 4.8 40.4 1.0 OE1 A:GLU234 4.8 54.7 1.0 O A:HOH633 4.9 36.4 1.0

L.A.Perera, C.Rato, Y.Yan, L.Neidhardt, S.H.Mclaughlin, R.J.Read, S.Preissler, D.Ron. An Oligomeric State-Dependent Switch in the Er Enzyme Ficd Regulates Ampylation and Deampylation of Bip. Embo J. V. 38 02177 2019.
ISSN: ESSN 1460-2075
PubMed: 31531998
DOI: 10.15252/EMBJ.2019102177