Atomistry » Zinc » PDB 3ad9-3ave » 3ahv
Atomistry »
  Zinc »
    PDB 3ad9-3ave »
      3ahv »

Zinc in PDB 3ahv: Semi-Active E176Q Mutant of Rice BGLU1 Covalent Complex with 2-Deoxy- 2-Fluoroglucoside

Enzymatic activity of Semi-Active E176Q Mutant of Rice BGLU1 Covalent Complex with 2-Deoxy- 2-Fluoroglucoside

All present enzymatic activity of Semi-Active E176Q Mutant of Rice BGLU1 Covalent Complex with 2-Deoxy- 2-Fluoroglucoside:
3.2.1.21;

Protein crystallography data

The structure of Semi-Active E176Q Mutant of Rice BGLU1 Covalent Complex with 2-Deoxy- 2-Fluoroglucoside, PDB code: 3ahv was solved by W.Chuenchor, S.Pengthaisong, R.C.Robinson, J.Yuvaniyama, J.Svasti, J.R.Ketudat Cairns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.75 / 1.89
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 79.226, 100.387, 127.407, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 21.3

Other elements in 3ahv:

The structure of Semi-Active E176Q Mutant of Rice BGLU1 Covalent Complex with 2-Deoxy- 2-Fluoroglucoside also contains other interesting chemical elements:

Fluorine (F) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Semi-Active E176Q Mutant of Rice BGLU1 Covalent Complex with 2-Deoxy- 2-Fluoroglucoside (pdb code 3ahv). 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 Semi-Active E176Q Mutant of Rice BGLU1 Covalent Complex with 2-Deoxy- 2-Fluoroglucoside, PDB code: 3ahv:

Zinc binding site 1 out of 1 in 3ahv

Go back to Zinc Binding Sites List in 3ahv
Zinc binding site 1 out of 1 in the Semi-Active E176Q Mutant of Rice BGLU1 Covalent Complex with 2-Deoxy- 2-Fluoroglucoside


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Semi-Active E176Q Mutant of Rice BGLU1 Covalent Complex with 2-Deoxy- 2-Fluoroglucoside within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:10.2
occ:1.00
 OD2 B:ASP65 2.0 11.1 1.0
ND1 B:HIS68 2.0 12.4 1.0
OD2 A:ASP65 2.0 11.2 1.0
ND1 A:HIS68 2.1 11.9 1.0
CG B:ASP65 2.7 9.7 1.0
CG A:ASP65 2.7 9.4 1.0
OD1 B:ASP65 2.8 9.6 1.0
OD1 A:ASP65 2.8 10.0 1.0
CG B:HIS68 3.0 9.2 1.0
CE1 B:HIS68 3.0 11.1 1.0
CE1 A:HIS68 3.0 10.6 1.0
CG A:HIS68 3.1 9.6 1.0
CB B:HIS68 3.4 9.5 1.0
CB A:HIS68 3.4 9.2 1.0
NE2 B:HIS68 4.1 9.9 1.0
O A:HOH606 4.1 19.1 1.0
CD2 B:HIS68 4.1 11.5 1.0
O B:HOH647 4.1 18.9 1.0
NE2 A:HIS68 4.2 10.5 1.0
CD2 A:HIS68 4.2 10.9 1.0
CB B:ASP65 4.2 8.8 1.0
CB A:ASP65 4.2 9.0 1.0
O B:HOH569 4.7 16.4 1.0
O A:HOH538 4.7 13.7 1.0
CA B:HIS68 4.8 10.2 1.0
CA A:HIS68 4.8 10.4 1.0
N B:HIS68 5.0 10.1 1.0

Reference:

W.Chuenchor, S.Pengthaisong, R.C.Robinson, J.Yuvaniyama, J.Svasti, J.R.Ketudat Cairns. The Structural Basis of Oligosaccharide Binding By Rice BGLU1 Beta-Glucosidase J.Struct.Biol. V. 173 169 2011.
ISSN: ISSN 1047-8477
PubMed: 20884352
DOI: 10.1016/J.JSB.2010.09.021
Page generated: Thu Oct 24 11:12:20 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy