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Zinc in PDB 3dx1: Golgi Alpha-Mannosidase II in Complex with Mannostatin Analog (1S,2S, 3R,4R)-4-Aminocyclopentane-1,2,3-Triol

Enzymatic activity of Golgi Alpha-Mannosidase II in Complex with Mannostatin Analog (1S,2S, 3R,4R)-4-Aminocyclopentane-1,2,3-Triol

All present enzymatic activity of Golgi Alpha-Mannosidase II in Complex with Mannostatin Analog (1S,2S, 3R,4R)-4-Aminocyclopentane-1,2,3-Triol:
3.2.1.114;

Protein crystallography data

The structure of Golgi Alpha-Mannosidase II in Complex with Mannostatin Analog (1S,2S, 3R,4R)-4-Aminocyclopentane-1,2,3-Triol, PDB code: 3dx1 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) 20.00 / 1.21
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.917, 109.539, 138.689, 90.00, 90.00, 90.00
R / Rfree (%) 12.7 / 16.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Golgi Alpha-Mannosidase II in Complex with Mannostatin Analog (1S,2S, 3R,4R)-4-Aminocyclopentane-1,2,3-Triol (pdb code 3dx1). 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 in Complex with Mannostatin Analog (1S,2S, 3R,4R)-4-Aminocyclopentane-1,2,3-Triol, PDB code: 3dx1:

Zinc binding site 1 out of 1 in 3dx1

Go back to Zinc Binding Sites List in 3dx1
Zinc binding site 1 out of 1 in the Golgi Alpha-Mannosidase II in Complex with Mannostatin Analog (1S,2S, 3R,4R)-4-Aminocyclopentane-1,2,3-Triol


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 in Complex with Mannostatin Analog (1S,2S, 3R,4R)-4-Aminocyclopentane-1,2,3-Triol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1048

b:9.7
occ:1.00
 NE2 A:HIS90 2.1 8.9 1.0
OD2 A:ASP204 2.1 9.7 1.0
NE2 A:HIS471 2.1 7.7 1.0
OD1 A:ASP92 2.1 9.3 1.0
O3 A:YHO1050 2.1 9.2 1.0
O2 A:YHO1050 2.2 10.8 1.0
CD2 A:HIS90 3.0 9.6 1.0
CG A:ASP92 3.1 9.4 1.0
CD2 A:HIS471 3.1 7.8 1.0
CE1 A:HIS90 3.1 9.0 1.0
CE1 A:HIS471 3.1 7.7 1.0
C2 A:YHO1050 3.1 10.6 1.0
C3 A:YHO1050 3.2 9.3 1.0
CG A:ASP204 3.2 8.7 1.0
OD2 A:ASP92 3.4 11.5 1.0
CB A:ASP204 3.6 8.9 1.0
N1 A:YHO1050 3.9 12.3 1.0
C1 A:YHO1050 4.0 11.3 1.0
OD2 A:ASP472 4.1 8.8 1.0
C5 A:YHO1050 4.2 11.7 1.0
CG A:HIS90 4.2 9.5 1.0
OD1 A:ASP204 4.2 10.0 1.0
ND1 A:HIS90 4.2 9.2 1.0
ND1 A:HIS471 4.3 7.5 1.0
CG A:HIS471 4.3 7.9 1.0
C4 A:YHO1050 4.3 10.2 1.0
CB A:ASP92 4.4 9.8 1.0
CE1 A:HIS470 4.5 8.9 1.0
OH A:TYR269 4.7 16.7 1.0
O A:HOH2368 4.7 12.3 1.0
O4 A:YHO1050 4.9 10.2 1.0

Reference:

D.A.Kuntz, W.Zhong, J.Guo, D.R.Rose, G.J.Boons. The Molecular Basis of Inhibition of Golgi Alpha-Mannosidase II By Mannostatin A. Chembiochem V. 10 268 2009.
ISSN: ISSN 1439-4227
PubMed: 19101978
DOI: 10.1002/CBIC.200800538
Page generated: Thu Oct 24 12:21:41 2024

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