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Zinc in PDB 3buq: Golgi Alpha-Mannosidase II D204A Catalytic Nucleophile Mutant with Bound Mannose.

Enzymatic activity of Golgi Alpha-Mannosidase II D204A Catalytic Nucleophile Mutant with Bound Mannose.

All present enzymatic activity of Golgi Alpha-Mannosidase II D204A Catalytic Nucleophile Mutant with Bound Mannose.:
3.2.1.114;

Protein crystallography data

The structure of Golgi Alpha-Mannosidase II D204A Catalytic Nucleophile Mutant with Bound Mannose., PDB code: 3buq 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) 16.52 / 2.01
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.607, 109.508, 138.607, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 17.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Golgi Alpha-Mannosidase II D204A Catalytic Nucleophile Mutant with Bound Mannose. (pdb code 3buq). 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 D204A Catalytic Nucleophile Mutant with Bound Mannose., PDB code: 3buq:

Zinc binding site 1 out of 1 in 3buq

Go back to Zinc Binding Sites List in 3buq
Zinc binding site 1 out of 1 in the Golgi Alpha-Mannosidase II D204A Catalytic Nucleophile Mutant with Bound Mannose.


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 D204A Catalytic Nucleophile Mutant with Bound Mannose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1048

b:15.0
occ:1.00
OD1 A:ASP92 2.0 11.7 1.0
NE2 A:HIS90 2.0 8.5 1.0
NE2 A:HIS471 2.0 10.8 1.0
O3 A:MAN1047 2.2 14.9 1.0
O2 A:MAN1047 2.5 17.1 1.0
C2 A:MAN1047 2.9 18.6 1.0
CG A:ASP92 2.9 10.8 1.0
CD2 A:HIS90 3.0 8.9 1.0
CE1 A:HIS471 3.0 8.2 1.0
C3 A:MAN1047 3.0 16.0 1.0
CE1 A:HIS90 3.0 8.6 1.0
CD2 A:HIS471 3.1 8.7 1.0
OD2 A:ASP92 3.2 11.9 1.0
CB A:ALA204 3.9 7.8 1.0
OD2 A:ASP472 3.9 10.4 1.0
ND1 A:HIS471 4.1 9.8 1.0
ND1 A:HIS90 4.1 10.4 1.0
CG A:HIS90 4.1 9.1 1.0
C4 A:MAN1047 4.2 15.2 1.0
CG A:HIS471 4.2 10.1 1.0
CE1 A:HIS470 4.2 9.0 1.0
CB A:ASP92 4.3 9.5 1.0
C1 A:MAN1047 4.4 19.0 1.0
O A:HOH1755 4.5 11.0 1.0
OH A:TYR269 4.6 11.4 1.0
CA A:ASP92 4.8 9.6 1.0
NE2 A:HIS470 4.9 10.3 1.0
O4 A:MAN1047 4.9 12.6 1.0
CG A:ASP472 5.0 9.4 1.0

Reference:

W.Zhong, D.A.Kuntz, B.Ember, H.Singh, K.W.Moremen, D.R.Rose, G.J.Boons. Probing the Substrate Specificity of Golgi Alpha-Mannosidase II By Use of Synthetic Oligosaccharides and A Catalytic Nucleophile Mutant. J.Am.Chem.Soc. V. 130 8975 2008.
ISSN: ISSN 0002-7863
PubMed: 18558690
DOI: 10.1021/JA711248Y
Page generated: Wed Aug 20 08:04:55 2025

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