Atomistry » Magnesium » PDB 6u1j-6uey » 6u4b
Atomistry »
  Magnesium »
    PDB 6u1j-6uey »
      6u4b »

Magnesium in PDB 6u4b: Wbbm Bifunctional Glycosytransferase Apo Structure

Protein crystallography data

The structure of Wbbm Bifunctional Glycosytransferase Apo Structure, PDB code: 6u4b was solved by M.S.Kimber, E.Mallette, E.R.Kamski-Hennekam, R.Gitalis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.28 / 2.10
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 124.030, 124.030, 73.050, 90.00, 90.00, 120.00
R / Rfree (%) 18.8 / 22.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Wbbm Bifunctional Glycosytransferase Apo Structure (pdb code 6u4b). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Wbbm Bifunctional Glycosytransferase Apo Structure, PDB code: 6u4b:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6u4b

Go back to Magnesium Binding Sites List in 6u4b
Magnesium binding site 1 out of 2 in the Wbbm Bifunctional Glycosytransferase Apo Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Wbbm Bifunctional Glycosytransferase Apo Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:38.1
occ:0.33
O A:HOH718 2.1 40.2 1.0
OD1 A:ASN565 2.1 64.0 1.0
CG A:ASN565 3.0 57.6 1.0
ND2 A:ASN565 3.4 56.0 1.0
OE1 A:GLU569 4.2 61.7 1.0
OE2 A:GLU569 4.2 60.0 1.0
CB A:ASN565 4.3 54.4 1.0
N A:ASN565 4.6 44.5 1.0
CA A:ASN565 4.6 44.4 1.0
CD A:GLU569 4.7 60.9 1.0

Magnesium binding site 2 out of 2 in 6u4b

Go back to Magnesium Binding Sites List in 6u4b
Magnesium binding site 2 out of 2 in the Wbbm Bifunctional Glycosytransferase Apo Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Wbbm Bifunctional Glycosytransferase Apo Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg602

b:35.9
occ:1.00
NE2 A:HIS540 2.1 60.2 1.0
OD2 A:ASP386 2.1 49.8 1.0
OD1 A:ASP388 2.5 47.3 1.0
OD2 A:ASP388 2.7 51.0 1.0
O A:HOH866 2.8 49.5 1.0
CE1 A:HIS540 2.9 58.8 1.0
CG A:ASP388 3.0 48.3 1.0
CG A:ASP386 3.1 44.9 1.0
CD2 A:HIS540 3.1 56.0 1.0
CB A:ASP386 3.5 36.9 1.0
ND1 A:HIS540 4.1 58.0 1.0
OD1 A:ASP386 4.2 45.9 1.0
CG A:HIS540 4.2 55.5 1.0
CB A:ALA542 4.3 69.9 1.0
CB A:ASP388 4.5 46.5 1.0
CA A:ALA542 4.5 71.9 1.0
O A:HOH861 4.9 54.8 1.0
CA A:ASP386 4.9 33.7 1.0
N A:ALA542 5.0 63.9 1.0

Reference:

B.R.Clarke, B.T.Sweeney, S.D.Kelly, O.G.Ovchinnikova, E.Mallette, T.E.Lowary, M.S.Kimber, C.Whitfield. Structure of the Bifunctional O-Antigen Polymerase From Klebsiella Pneumoniae Reveals A New Family of Galactofuranosyltransferases To Be Published.
Page generated: Tue Oct 1 20:49:46 2024

Last articles

Zn in 1ALN
Zn in 1ALJ
Zn in 1AJY
Zn in 1ALH
Zn in 1AK0
Zn in 1AKL
Zn in 1AJD
Zn in 1AJC
Zn in 1AJB
Zn in 1AIY
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy