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Magnesium in PDB 3zcb: Vbht Fic Protein From Bartonella Schoenbuchensis in Complex with Vbha Antitoxin Mutant E24G and Atp

Protein crystallography data

The structure of Vbht Fic Protein From Bartonella Schoenbuchensis in Complex with Vbha Antitoxin Mutant E24G and Atp, PDB code: 3zcb was solved by A.Goepfert, T.Schirmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.94
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 106.460, 40.250, 73.900, 90.00, 121.38, 90.00
R / Rfree (%) 19.51 / 24.931

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Vbht Fic Protein From Bartonella Schoenbuchensis in Complex with Vbha Antitoxin Mutant E24G and Atp (pdb code 3zcb). 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 Vbht Fic Protein From Bartonella Schoenbuchensis in Complex with Vbha Antitoxin Mutant E24G and Atp, PDB code: 3zcb:

Magnesium binding site 1 out of 1 in 3zcb

Go back to Magnesium Binding Sites List in 3zcb
Magnesium binding site 1 out of 1 in the Vbht Fic Protein From Bartonella Schoenbuchensis in Complex with Vbha Antitoxin Mutant E24G and Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Vbht Fic Protein From Bartonella Schoenbuchensis in Complex with Vbha Antitoxin Mutant E24G and Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:11.4
occ:1.00
OE1 A:GLU140 1.9 22.9 1.0
O1A A:ATP300 2.0 16.4 1.0
O2B A:ATP300 2.0 16.6 1.0
O A:HOH2062 2.1 31.6 1.0
O A:HOH2089 2.2 30.0 1.0
O A:HOH2109 2.2 34.1 1.0
CD A:GLU140 2.9 22.2 1.0
PA A:ATP300 3.1 14.5 1.0
PB A:ATP300 3.1 16.1 1.0
OE2 A:GLU140 3.2 24.5 1.0
O3A A:ATP300 3.4 17.1 1.0
O3B A:ATP300 3.5 21.3 1.0
O2A A:ATP300 3.8 14.4 1.0
NH2 A:ARG144 4.1 15.1 1.0
N A:GLY141 4.1 15.3 1.0
O2 A:GOL1199 4.2 34.0 1.0
CG A:GLU140 4.3 20.8 1.0
O A:HOH2016 4.4 48.4 1.0
O1B A:ATP300 4.4 15.6 1.0
O5' A:ATP300 4.5 18.3 1.0
CB A:GLU140 4.7 19.1 1.0
CA A:GLU140 4.8 17.4 1.0
C2 A:GOL1199 4.9 38.8 1.0
CA A:GLY141 4.9 14.7 1.0
O A:HOH2063 5.0 33.9 1.0

Reference:

A.Goepfert, F.V.Stanger, C.Dehio, T.Schirmer. Conserved Inhibitory Mechanism and Competent Atp Binding Mode For Adenylyltransferases with Fic Fold. Plos One V. 8 64901 2013.
ISSN: ISSN 1932-6203
PubMed: 23738009
DOI: 10.1371/JOURNAL.PONE.0064901
Page generated: Mon Dec 14 09:02:54 2020

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