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Magnesium in PDB 4m2a: Crystal Structure of the Udp-Glucose Pyrophosphorylase From Leishmania Major in the Post-Reactive State

Enzymatic activity of Crystal Structure of the Udp-Glucose Pyrophosphorylase From Leishmania Major in the Post-Reactive State

All present enzymatic activity of Crystal Structure of the Udp-Glucose Pyrophosphorylase From Leishmania Major in the Post-Reactive State:
2.7.7.9;

Protein crystallography data

The structure of Crystal Structure of the Udp-Glucose Pyrophosphorylase From Leishmania Major in the Post-Reactive State, PDB code: 4m2a was solved by J.Fuehring, F.H.Routier, A.-C.Lamerz, P.Baruch, R.Gerardy-Schahn, R.Fedorov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.60 / 1.66
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 79.790, 89.090, 136.490, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 25

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Udp-Glucose Pyrophosphorylase From Leishmania Major in the Post-Reactive State (pdb code 4m2a). 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 the Udp-Glucose Pyrophosphorylase From Leishmania Major in the Post-Reactive State, PDB code: 4m2a:

Magnesium binding site 1 out of 1 in 4m2a

Go back to Magnesium Binding Sites List in 4m2a
Magnesium binding site 1 out of 1 in the Crystal Structure of the Udp-Glucose Pyrophosphorylase From Leishmania Major in the Post-Reactive State


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 the Udp-Glucose Pyrophosphorylase From Leishmania Major in the Post-Reactive State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1002

b:30.5
occ:1.00
 O4 A:SO41003 2.6 44.3 1.0
O A:HOH2549 2.8 44.0 1.0
O2A A:UPG1001 2.9 12.6 1.0
S A:SO41003 3.4 50.6 1.0
C6 A:UPG1001 3.5 12.5 1.0
O2 A:SO41003 3.5 42.1 1.0
CA A:GLY84 3.6 22.5 1.0
PA A:UPG1001 3.7 13.0 1.0
O5C A:UPG1001 3.7 11.8 1.0
C2C A:UPG1001 3.7 11.9 1.0
O1 A:SO41003 3.7 43.6 1.0
O A:HOH2240 3.8 20.9 1.0
N A:LEU85 3.9 28.1 1.0
O A:HOH2524 3.9 41.0 1.0
C5 A:UPG1001 4.0 11.8 1.0
O A:HOH2502 4.0 23.1 1.0
O2C A:UPG1001 4.1 11.4 1.0
O1A A:UPG1001 4.1 13.9 1.0
C A:GLY84 4.2 24.6 1.0
O A:HOH2585 4.2 30.4 1.0
N1 A:UPG1001 4.3 11.6 1.0
C1C A:UPG1001 4.5 10.6 1.0
N A:GLY84 4.6 17.5 1.0
N A:GLY86 4.6 37.4 1.0
O A:HOH2547 4.6 35.4 1.0
C3C A:UPG1001 4.6 12.4 1.0
O A:HOH2548 4.7 24.8 1.0
O3 A:SO41003 4.8 47.1 1.0
O4C A:UPG1001 5.0 11.1 1.0
C5C A:UPG1001 5.0 10.6 1.0

Reference:

J.Fuehring, F.H.Routier, A.-C.Lamerz, P.Baruch, R.Gerardy-Schahn, R.Fedorov. Catalytic Mechanism and Allosteric Regulation of Udp-Glucose Pyrophosphorylase From Leishmania Major Acs Catalysis V. 3 2161 2013.
ISSN: ESSN 2155-5435
DOI: 10.1021/CS4007777
Page generated: Mon Dec 14 19:11:22 2020

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