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Zinc in PDB 1qx1: Golgi Alpha-Mannosidase II D341N Mutant Complex with 2-F-Mannosyl-F

Enzymatic activity of Golgi Alpha-Mannosidase II D341N Mutant Complex with 2-F-Mannosyl-F

All present enzymatic activity of Golgi Alpha-Mannosidase II D341N Mutant Complex with 2-F-Mannosyl-F:
3.2.1.114;

Protein crystallography data

The structure of Golgi Alpha-Mannosidase II D341N Mutant Complex with 2-F-Mannosyl-F, PDB code: 1qx1 was solved by S.Numao, D.A.Kuntz, S.G.Withers, D.R.Rose, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.23 / 1.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.046, 109.826, 138.907, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 18.9

Other elements in 1qx1:

The structure of Golgi Alpha-Mannosidase II D341N Mutant Complex with 2-F-Mannosyl-F also contains other interesting chemical elements:

Fluorine (F) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Golgi Alpha-Mannosidase II D341N Mutant Complex with 2-F-Mannosyl-F (pdb code 1qx1). 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 Alpha-Mannosidase II D341N Mutant Complex with 2-F-Mannosyl-F, PDB code: 1qx1:

Zinc binding site 1 out of 1 in 1qx1

Go back to Zinc Binding Sites List in 1qx1
Zinc binding site 1 out of 1 in the Golgi Alpha-Mannosidase II D341N Mutant Complex with 2-F-Mannosyl-F


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Golgi Alpha-Mannosidase II D341N Mutant Complex with 2-F-Mannosyl-F within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2004

b:12.9
occ:1.00
OD1 A:ASP92 2.0 13.0 1.0
NE2 A:HIS90 2.1 9.8 1.0
O3 A:FMF2003 2.1 6.7 0.5
NE2 A:HIS471 2.1 6.7 1.0
O3 A:FMF2003 2.2 21.9 0.5
F2 A:FMF2003 2.5 18.1 0.5
F2 A:FMF2003 2.6 14.0 0.5
OD1 A:ASP204 2.7 11.4 1.0
CG A:ASP92 2.9 14.0 1.0
CE1 A:HIS90 3.0 8.3 1.0
CE1 A:HIS471 3.1 9.3 1.0
CD2 A:HIS471 3.1 7.1 1.0
CD2 A:HIS90 3.1 10.0 1.0
OD2 A:ASP92 3.1 16.7 1.0
C2 A:FMF2003 3.2 14.3 0.5
C3 A:FMF2003 3.2 11.6 0.5
C3 A:FMF2003 3.3 14.1 0.5
C2 A:FMF2003 3.3 12.7 0.5
C1 A:FMF2003 3.6 14.2 0.5
CG A:ASP204 3.6 9.9 1.0
CB A:ASP204 3.8 10.2 1.0
OD2 A:ASP472 3.9 9.3 1.0
C1 A:FMF2003 4.0 14.6 0.5
ND1 A:HIS90 4.2 10.7 1.0
NE2 A:HIS470 4.2 13.3 1.0
ND1 A:HIS471 4.2 8.1 1.0
CG A:HIS90 4.2 8.8 1.0
CB A:ASP92 4.2 11.5 1.0
CG A:HIS471 4.2 7.3 1.0
C4 A:FMF2003 4.3 13.6 0.5
C4 A:FMF2003 4.3 11.5 0.5
O A:HOH2095 4.5 11.6 1.0
CA A:ASP92 4.7 10.2 1.0
OD2 A:ASP204 4.8 10.6 1.0
O A:FMF2003 4.8 13.0 0.5
O A:HOH2894 4.8 22.9 1.0
O A:FMF2003 4.8 17.1 0.5
CE1 A:HIS470 4.8 6.7 1.0
CG A:ASP472 4.9 8.0 1.0

Reference:

S.Numao, D.A.Kuntz, S.G.Withers, D.R.Rose. Insights Into the Mechanism of Drosophila Melanogaster Golgi Alpha-Mannosidase II Through the Structural Analysis of Covalent Reaction Intermediates. J.Biol.Chem. V. 278 48074 2003.
ISSN: ISSN 0021-9258
PubMed: 12960159
DOI: 10.1074/JBC.M309249200
Page generated: Mon Jan 25 16:12:30 2021

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