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Magnesium in PDB 3tvk: Diguanylate Cyclase Domain of Dgcz

Enzymatic activity of Diguanylate Cyclase Domain of Dgcz

All present enzymatic activity of Diguanylate Cyclase Domain of Dgcz:
2.7.7.65;

Protein crystallography data

The structure of Diguanylate Cyclase Domain of Dgcz, PDB code: 3tvk was solved by F.Zaehringer, T.Schirmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.80
Space group P 62
Cell size a, b, c (Å), α, β, γ (°) 79.623, 79.623, 51.207, 90.00, 90.00, 120.00
R / Rfree (%) 16.6 / 20.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Diguanylate Cyclase Domain of Dgcz (pdb code 3tvk). 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 Diguanylate Cyclase Domain of Dgcz, PDB code: 3tvk:

Magnesium binding site 1 out of 1 in 3tvk

Go back to Magnesium Binding Sites List in 3tvk
Magnesium binding site 1 out of 1 in the Diguanylate Cyclase Domain of Dgcz


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Diguanylate Cyclase Domain of Dgcz within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg504

b:29.6
occ:1.00
O A:HOH723 2.0 25.0 1.0
O A:HOH680 2.0 26.3 1.0
O1P A:C2E502 2.0 14.1 1.0
OD2 A:ASP198 2.2 23.4 1.0
O A:HOH678 2.2 23.6 1.0
O A:HOH685 2.3 27.7 1.0
CG A:ASP198 3.1 27.9 1.0
P1 A:C2E502 3.4 13.5 1.0
OD1 A:ASP198 3.5 29.5 1.0
O3A A:C2E502 3.8 12.3 1.0
O A:HOH615 4.0 14.1 1.0
C5' A:C2E502 4.2 12.8 1.0
O A:HOH675 4.2 22.8 1.0
O5' A:C2E502 4.3 14.4 1.0
N A:ASP198 4.4 23.1 1.0
CB A:ASP198 4.4 25.8 1.0
O A:THR196 4.4 13.6 1.0
O A:HOH736 4.5 32.5 1.0
O2P A:C2E502 4.5 13.4 1.0
O A:HOH676 4.5 18.8 1.0
CA A:ASP198 4.7 21.9 1.0
C A:ARG197 5.0 18.0 1.0

Reference:

F.Zahringer, E.Lacanna, U.Jenal, T.Schirmer, A.Boehm. Structure and Signaling Mechanism of A Zinc-Sensory Diguanylate Cyclase. Structure V. 21 1149 2013.
ISSN: ISSN 0969-2126
PubMed: 23769666
DOI: 10.1016/J.STR.2013.04.026
Page generated: Mon Aug 11 04:00:28 2025

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