Atomistry » Zinc » PDB 3bof-3c52 » 3bui
Atomistry »
  Zinc »
    PDB 3bof-3c52 »
      3bui »

Zinc in PDB 3bui: Golgi Mannosidase II D204A Catalytic Nucleophile Mutant Complex with Tris

Enzymatic activity of Golgi Mannosidase II D204A Catalytic Nucleophile Mutant Complex with Tris

All present enzymatic activity of Golgi Mannosidase II D204A Catalytic Nucleophile Mutant Complex with Tris:
3.2.1.114;

Protein crystallography data

The structure of Golgi Mannosidase II D204A Catalytic Nucleophile Mutant Complex with Tris, PDB code: 3bui was solved by D.A.Kuntz, D.R.Rose, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.25
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.259, 108.988, 137.569, 90.00, 90.00, 90.00
R / Rfree (%) 12.1 / 15.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Golgi Mannosidase II D204A Catalytic Nucleophile Mutant Complex with Tris (pdb code 3bui). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Golgi Mannosidase II D204A Catalytic Nucleophile Mutant Complex with Tris, PDB code: 3bui:

Zinc binding site 1 out of 1 in 3bui

Go back to Zinc Binding Sites List in 3bui
Zinc binding site 1 out of 1 in the Golgi Mannosidase II D204A Catalytic Nucleophile Mutant Complex with Tris


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Golgi Mannosidase II D204A Catalytic Nucleophile Mutant Complex with Tris within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1046

b:7.9
occ:1.00
OD1 A:ASP92 2.0 8.2 1.0
NE2 A:HIS90 2.0 7.4 1.0
NE2 A:HIS471 2.0 6.4 1.0
O3 A:TRS1047 2.1 12.9 1.0
N A:TRS1047 2.1 16.7 1.0
O1 A:TRS1047 2.4 15.5 0.6
CG A:ASP92 2.8 7.7 1.0
CD2 A:HIS90 3.0 8.3 1.0
CE1 A:HIS471 3.0 6.8 1.0
C A:TRS1047 3.0 13.6 1.0
C3 A:TRS1047 3.0 16.7 1.0
CE1 A:HIS90 3.1 7.8 1.0
OD2 A:ASP92 3.1 10.7 1.0
CD2 A:HIS471 3.1 6.2 1.0
C1 A:TRS1047 3.3 15.4 1.0
CB A:ALA204 3.9 9.2 1.0
OD2 A:ASP472 3.9 8.7 1.0
CG A:HIS90 4.1 7.3 1.0
ND1 A:HIS471 4.2 6.2 1.0
ND1 A:HIS90 4.2 7.1 1.0
CG A:HIS471 4.2 6.1 1.0
CB A:ASP92 4.2 7.2 1.0
CE1 A:HIS470 4.2 7.2 1.0
C2 A:TRS1047 4.4 16.2 1.0
O A:HOH1720 4.4 10.3 1.0
O1 A:TRS1047 4.5 11.2 0.5
OH A:TYR269 4.6 9.8 1.0
CA A:ASP92 4.7 6.6 1.0
NE2 A:HIS470 4.8 7.4 1.0

Reference:

W.Zhong, D.A.Kuntz, B.Ember, H.Singh, K.W.Moremen, D.R.Rose, G.J.Boons. Probing the Substrate Specificity of Golgi Alpha-Mannosidase II By Use of Synthetic Oligosaccharides and A Catalytic Nucleophile Mutant. J.Am.Chem.Soc. V. 130 8975 2008.
ISSN: ISSN 0002-7863
PubMed: 18558690
DOI: 10.1021/JA711248Y
Page generated: Wed Aug 20 08:04:41 2025

Last articles

Zn in 3RZU
Zn in 3S0Z
Zn in 3RZO
Zn in 3RZD
Zn in 3S0N
Zn in 3RZV
Zn in 3RYM
Zn in 3RZA
Zn in 3RZ8
Zn in 3RZ7
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy