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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

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