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Zinc in PDB 3d52: Golgi Mannosidase II Complex with An N-Aryl Carbamate Derivative of Gluco-Hydroxyiminolactam

Enzymatic activity of Golgi Mannosidase II Complex with An N-Aryl Carbamate Derivative of Gluco-Hydroxyiminolactam

All present enzymatic activity of Golgi Mannosidase II Complex with An N-Aryl Carbamate Derivative of Gluco-Hydroxyiminolactam:
3.2.1.114;

Protein crystallography data

The structure of Golgi Mannosidase II Complex with An N-Aryl Carbamate Derivative of Gluco-Hydroxyiminolactam, PDB code: 3d52 was solved by D.A.Kuntz, C.A.Tarling, 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) 19.72 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.579, 107.912, 137.062, 90.00, 90.00, 90.00
R / Rfree (%) 22.8 / 24

Other elements in 3d52:

The structure of Golgi Mannosidase II Complex with An N-Aryl Carbamate Derivative of Gluco-Hydroxyiminolactam also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Golgi Mannosidase II Complex with An N-Aryl Carbamate Derivative of Gluco-Hydroxyiminolactam (pdb code 3d52). 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 Mannosidase II Complex with An N-Aryl Carbamate Derivative of Gluco-Hydroxyiminolactam, PDB code: 3d52:

Zinc binding site 1 out of 1 in 3d52

Go back to Zinc Binding Sites List in 3d52
Zinc binding site 1 out of 1 in the Golgi Mannosidase II Complex with An N-Aryl Carbamate Derivative of Gluco-Hydroxyiminolactam


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Golgi Mannosidase II Complex with An N-Aryl Carbamate Derivative of Gluco-Hydroxyiminolactam within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1046

b:10.0
occ:1.00
 OD2 A:ASP204 2.1 10.8 1.0
NE2 A:HIS90 2.1 9.5 1.0
OD1 A:ASP92 2.1 9.0 1.0
NE2 A:HIS471 2.1 8.0 1.0
O3 A:GHR1048 2.3 7.9 1.0
O2 A:GHR1048 2.5 12.2 1.0
C2 A:GHR1048 3.0 9.3 1.0
CG A:ASP92 3.0 8.7 1.0
CE1 A:HIS90 3.1 8.5 1.0
CD2 A:HIS471 3.1 10.2 1.0
CD2 A:HIS90 3.1 10.2 1.0
CG A:ASP204 3.1 11.0 1.0
CE1 A:HIS471 3.1 6.4 1.0
C3 A:GHR1048 3.2 8.1 1.0
OD2 A:ASP92 3.4 12.1 1.0
CB A:ASP204 3.5 7.6 1.0
OD2 A:ASP472 4.0 8.5 1.0
ND1 A:HIS90 4.2 8.5 1.0
OD1 A:ASP204 4.2 12.1 1.0
CG A:HIS471 4.2 6.7 1.0
CG A:HIS90 4.2 7.8 1.0
ND1 A:HIS471 4.2 7.0 1.0
C4 A:GHR1048 4.3 8.3 1.0
CE1 A:HIS470 4.4 9.2 1.0
CB A:ASP92 4.4 8.4 1.0
C1 A:GHR1048 4.5 14.1 1.0
O A:HOH1700 4.6 10.9 1.0
OH A:TYR269 4.7 14.4 1.0
CA A:ASP92 4.9 7.1 1.0
CG A:ASP472 5.0 7.2 1.0

Reference:

D.A.Kuntz, C.A.Tarling, S.G.Withers, D.R.Rose. Structural Analysis of Golgi Alpha-Mannosidase II Inhibitors Identified From A Focused Glycosidase Inhibitor Screen. Biochemistry V. 47 10058 2008.
ISSN: ISSN 0006-2960
PubMed: 18759458
DOI: 10.1021/BI8010785
Page generated: Thu Oct 24 12:03:45 2024

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