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Zinc in PDB 3esw: Complex of Yeast Pngase with GLCNAC2-Iac.

Enzymatic activity of Complex of Yeast Pngase with GLCNAC2-Iac.

All present enzymatic activity of Complex of Yeast Pngase with GLCNAC2-Iac.:
3.5.1.52;

Protein crystallography data

The structure of Complex of Yeast Pngase with GLCNAC2-Iac., PDB code: 3esw was solved by G.Zhao, X.Zhou, W.J.Lennarz, H.Schindelin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.96 / 3.40
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 131.530, 131.530, 127.751, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / 23.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Complex of Yeast Pngase with GLCNAC2-Iac. (pdb code 3esw). 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 Complex of Yeast Pngase with GLCNAC2-Iac., PDB code: 3esw:

Zinc binding site 1 out of 1 in 3esw

Go back to Zinc Binding Sites List in 3esw
Zinc binding site 1 out of 1 in the Complex of Yeast Pngase with GLCNAC2-Iac.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Complex of Yeast Pngase with GLCNAC2-Iac. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn344

b:77.8
occ:1.00
SG A:CYS132 1.9 60.0 1.0
SG A:CYS168 2.2 51.7 1.0
SG A:CYS165 2.3 50.3 1.0
SG A:CYS129 2.4 60.0 1.0
CB A:CYS168 3.0 53.2 1.0
CB A:CYS132 3.2 62.9 1.0
CB A:CYS165 3.3 51.6 1.0
N A:CYS132 3.6 63.4 1.0
CB A:CYS129 3.7 58.0 1.0
CA A:CYS132 3.9 63.1 1.0
N A:CYS168 4.0 53.6 1.0
CA A:CYS168 4.0 53.2 1.0
ND1 A:HIS131 4.3 66.1 1.0
C A:ARG167 4.6 53.8 1.0
C A:HIS131 4.6 63.5 1.0
CA A:CYS165 4.8 51.7 1.0
C A:CYS168 4.8 53.4 1.0
CB A:HIS131 4.8 63.5 1.0
N A:GLY169 5.0 53.9 1.0
CA A:CYS129 5.0 58.1 1.0

Reference:

G.Zhao, G.Li, X.Zhou, I.Matsuo, Y.Ito, T.Suzuki, W.J.Lennarz, H.Schindelin. Structural and Mutational Studies on the Importance of Oligosaccharide Binding For the Activity of Yeast Pngase. Glycobiology V. 19 118 2009.
ISSN: ISSN 0959-6658
PubMed: 18854368
DOI: 10.1093/GLYCOB/CWN108
Page generated: Thu Oct 24 12:56:11 2024

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