Zinc in PDB 3hsu: Functional Roles of the 6-S-Cysteinyl, 8 Alpha-N1-Histidyl Fad in Glucooligosaccharide Oxidase From Acremonium Strictum

The structure of Functional Roles of the 6-S-Cysteinyl, 8 Alpha-N1-Histidyl Fad in Glucooligosaccharide Oxidase From Acremonium Strictum, PDB code: 3hsu was solved by S.-H.Liaw, C.-H.Huang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.88 / 1.69
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.483, 97.570, 98.200, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 22.8

The binding sites of Zinc atom in the Functional Roles of the 6-S-Cysteinyl, 8 Alpha-N1-Histidyl Fad in Glucooligosaccharide Oxidase From Acremonium Strictum (pdb code 3hsu). 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 Functional Roles of the 6-S-Cysteinyl, 8 Alpha-N1-Histidyl Fad in Glucooligosaccharide Oxidase From Acremonium Strictum, PDB code: 3hsu:

Zinc binding site 1 out of 1 in the Functional Roles of the 6-S-Cysteinyl, 8 Alpha-N1-Histidyl Fad in Glucooligosaccharide Oxidase From Acremonium Strictum


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Functional Roles of the 6-S-Cysteinyl, 8 Alpha-N1-Histidyl Fad in Glucooligosaccharide Oxidase From Acremonium Strictum within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn503 b:22.3 occ:1.00 OE1 A:GLU17 2.0 26.8 1.0 OD1 A:ASP36 2.1 23.6 1.0 OD2 A:ASP36 2.6 20.3 1.0 CG A:ASP36 2.7 22.3 1.0 CD A:GLU17 2.8 29.2 1.0 OE2 A:GLU17 2.9 29.5 1.0 O A:HOH875 4.0 43.3 1.0 O A:PRO37 4.1 19.2 1.0 CB A:ASP36 4.2 18.7 1.0 O A:HOH732 4.2 29.2 1.0 CG A:GLU17 4.2 28.6 1.0 CZ2 A:TRP22 4.5 23.3 1.0 CH2 A:TRP22 5.0 24.3 1.0

C.-H.Huang, A.Winkler, C.-L.Chen, W.-L.Lai, Y.-C.Tsai, P.Macheroux, S.-H.Liaw. Functional Roles of the 6-S-Cysteinyl, 8ALPHA-N1-Histidyl Fad in Glucooligosaccharide Oxidase From Acremonium Strictum J.Biol.Chem. V. 283 30990 2008.
ISSN: ISSN 0021-9258
PubMed: 18768475
DOI: 10.1074/JBC.M804331200