Atomistry » Magnesium » PDB 2cw0-2dkg » 2dgn
Atomistry »
  Magnesium »
    PDB 2cw0-2dkg »
      2dgn »

Magnesium in PDB 2dgn: Mouse Muscle Adenylosuccinate Synthetase Partially Ligated Complex with Gtp, 2'-Deoxy-Imp

Enzymatic activity of Mouse Muscle Adenylosuccinate Synthetase Partially Ligated Complex with Gtp, 2'-Deoxy-Imp

All present enzymatic activity of Mouse Muscle Adenylosuccinate Synthetase Partially Ligated Complex with Gtp, 2'-Deoxy-Imp:
6.3.4.4;

Protein crystallography data

The structure of Mouse Muscle Adenylosuccinate Synthetase Partially Ligated Complex with Gtp, 2'-Deoxy-Imp, PDB code: 2dgn was solved by C.V.Iancu, Y.Zhou, T.Borza, H.J.Fromm, R.B.Honzatko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.40
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 70.112, 70.112, 199.033, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 26.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mouse Muscle Adenylosuccinate Synthetase Partially Ligated Complex with Gtp, 2'-Deoxy-Imp (pdb code 2dgn). 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 Mouse Muscle Adenylosuccinate Synthetase Partially Ligated Complex with Gtp, 2'-Deoxy-Imp, PDB code: 2dgn:

Magnesium binding site 1 out of 1 in 2dgn

Go back to Magnesium Binding Sites List in 2dgn
Magnesium binding site 1 out of 1 in the Mouse Muscle Adenylosuccinate Synthetase Partially Ligated Complex with Gtp, 2'-Deoxy-Imp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mouse Muscle Adenylosuccinate Synthetase Partially Ligated Complex with Gtp, 2'-Deoxy-Imp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1454

b:19.2
occ:1.00
O16 A:DOI1451 2.0 29.1 1.0
O2B A:GDP1452 2.0 18.7 1.0
O2A A:GDP1452 2.1 28.2 1.0
O A:GLY70 2.1 26.3 1.0
O A:HOH513 2.2 23.2 1.0
OD1 A:ASP43 2.3 20.3 1.0
C A:GLY70 3.2 23.4 1.0
P6 A:DOI1451 3.2 38.2 1.0
PA A:GDP1452 3.4 24.5 1.0
PB A:GDP1452 3.4 19.6 1.0
CG A:ASP43 3.4 23.1 1.0
O36 A:DOI1451 3.5 27.5 1.0
O3A A:GDP1452 3.7 20.7 1.0
N A:GLY70 3.7 25.2 1.0
CA A:GLY70 3.8 23.6 1.0
CA A:ASP43 3.9 22.7 1.0
CD2 A:HIS71 4.0 24.7 1.0
CB A:ASP43 4.1 22.1 1.0
O26 A:DOI1451 4.1 30.6 1.0
N A:ASP43 4.1 18.9 1.0
N1 A:DOI1451 4.2 21.4 1.0
O1B A:GDP1452 4.2 10.6 1.0
N A:HIS71 4.3 21.7 1.0
O1A A:GDP1452 4.3 29.4 1.0
O6 A:DOI1451 4.4 25.6 1.0
O A:HOH579 4.4 34.1 1.0
O5' A:GDP1452 4.4 24.9 1.0
OD2 A:ASP43 4.4 21.4 1.0
O3B A:GDP1452 4.5 23.9 1.0
C6 A:DOI1451 4.6 22.8 1.0
CA A:HIS71 4.6 23.0 1.0
NE2 A:HIS71 4.8 27.7 1.0
O A:HOH592 4.9 38.7 1.0
C A:ALA69 5.0 24.4 1.0

Reference:

C.V.Iancu, Y.Zhou, T.Borza, H.J.Fromm, R.B.Honzatko. Cavitation As A Mechanism of Substrate Discrimination By Adenylosuccinate Synthetases. Biochemistry V. 45 11703 2006.
ISSN: ISSN 0006-2960
PubMed: 16981730
DOI: 10.1021/BI0607498
Page generated: Tue Aug 13 22:30:06 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy