Atomistry » Fluorine » PDB 1q6n-1rrx » 1qwu
Atomistry »
  Fluorine »
    PDB 1q6n-1rrx »
      1qwu »

Fluorine 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:

Zinc (Zn) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine 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 Fluorine atom.
In total only one binding site of Fluorine was determined in the Golgi Alpha-Mannosidase II D341N Mutant Complex with 5-F-Guloside, PDB code: 1qwu:

Fluorine binding site 1 out of 1 in 1qwu

Go back to Fluorine Binding Sites List in 1qwu
Fluorine 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 Fluorine with other atoms in the F 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:F2003

b:10.8
occ:1.00
 F1 A:GUL2003 0.0 10.8 1.0
C5 A:GUL2003 1.2 10.6 1.0
O A:GUL2003 2.2 9.7 1.0
C6 A:GUL2003 2.2 11.2 1.0
C4 A:GUL2003 2.4 9.7 1.0
O6 A:GUL2003 2.8 12.7 1.0
O4 A:GUL2003 2.9 10.6 1.0
CE1 A:PHE206 3.2 13.0 1.0
C1 A:GUL2003 3.3 11.9 1.0
NH2 A:ARG228 3.3 11.4 1.0
CZ3 A:TRP415 3.6 7.9 1.0
CH2 A:TRP415 3.7 8.5 1.0
C3 A:GUL2003 3.7 10.3 1.0
OD1 A:ASP204 3.7 11.9 1.0
CZ A:PHE206 3.8 11.9 1.0
CE2 A:TYR727 3.8 7.9 1.0
CD1 A:PHE206 3.9 11.1 1.0
CZ A:ARG228 3.9 13.6 1.0
OD2 A:ASP204 4.0 10.4 1.0
NE A:ARG228 4.0 11.9 1.0
C2 A:GUL2003 4.1 10.3 1.0
CG A:ASP204 4.1 13.0 1.0
OH A:TYR727 4.3 8.1 1.0
CZ A:TYR727 4.4 8.2 1.0
O A:ASP204 4.5 11.4 1.0
CD2 A:TYR727 4.5 7.4 1.0
O3 A:GUL2003 4.6 7.7 1.0
O A:HOH2875 4.8 16.7 1.0
NH1 A:ARG228 4.8 13.2 1.0
CE2 A:PHE206 4.8 12.2 1.0
CE3 A:TRP415 4.9 8.3 1.0
O A:ARG876 5.0 11.5 1.0
CG A:PHE206 5.0 12.1 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 Jul 31 12:33:42 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy