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Zinc in PDB 1qwu: Golgi Alpha-Mannosidase II D341N Mutant Complex with 5-F-Guloside

Enzymatic activity of Golgi Alpha-Mannosidase II D341N Mutant Complex with 5-F-Guloside

All present enzymatic activity of Golgi Alpha-Mannosidase II D341N Mutant Complex with 5-F-Guloside:
3.2.1.114;

Protein crystallography data

The structure of Golgi Alpha-Mannosidase II D341N Mutant Complex with 5-F-Guloside, PDB code: 1qwu 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) 19.84 / 2.03
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.850, 109.799, 138.765, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 18.9

Other elements in 1qwu:

The structure of Golgi Alpha-Mannosidase II D341N Mutant Complex with 5-F-Guloside also contains other interesting chemical elements:

Fluorine (F) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Golgi Alpha-Mannosidase II D341N Mutant Complex with 5-F-Guloside (pdb code 1qwu). 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 5-F-Guloside, PDB code: 1qwu:

Zinc binding site 1 out of 1 in 1qwu

Go back to Zinc Binding Sites List in 1qwu
Zinc binding site 1 out of 1 in the Golgi Alpha-Mannosidase II D341N Mutant Complex with 5-F-Guloside


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 5-F-Guloside within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2004

b:13.4
occ:1.00
 OD1 A:ASP92 2.0 13.2 1.0
NE2 A:HIS90 2.1 7.6 1.0
O3 A:GUL2003 2.1 7.7 1.0
NE2 A:HIS471 2.2 8.2 1.0
O2 A:GUL2003 2.3 9.0 1.0
OD1 A:ASP204 2.7 11.9 1.0
C2 A:GUL2003 2.9 10.3 1.0
CG A:ASP92 2.9 12.5 1.0
CD2 A:HIS90 3.0 6.6 1.0
C3 A:GUL2003 3.0 10.3 1.0
CD2 A:HIS471 3.1 8.3 1.0
CE1 A:HIS90 3.2 9.1 1.0
OD2 A:ASP92 3.2 12.9 1.0
CE1 A:HIS471 3.2 8.8 1.0
C1 A:GUL2003 3.3 11.9 1.0
CG A:ASP204 3.5 13.0 1.0
CB A:ASP204 3.7 10.9 1.0
OD2 A:ASP472 4.0 9.2 1.0
C4 A:GUL2003 4.1 9.7 1.0
CG A:HIS90 4.1 7.2 1.0
ND1 A:HIS90 4.2 8.9 1.0
CE1 A:HIS470 4.2 8.9 1.0
CG A:HIS471 4.3 7.8 1.0
CB A:ASP92 4.3 9.8 1.0
ND1 A:HIS471 4.3 8.7 1.0
O A:GUL2003 4.6 9.7 1.0
O A:HOH2096 4.6 11.4 1.0
OD2 A:ASP204 4.7 10.4 1.0
NE2 A:HIS470 4.8 8.6 1.0
CA A:ASP92 4.8 11.4 1.0
CG A:ASP472 5.0 9.6 1.0
C5 A:GUL2003 5.0 10.6 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: Wed Oct 16 18:17:41 2024

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