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Zinc in PDB 4qlk: Crystal Structure of Rice BGLU1 E176Q/Y341A Mutant Complexed with Cellotetraose

Enzymatic activity of Crystal Structure of Rice BGLU1 E176Q/Y341A Mutant Complexed with Cellotetraose

All present enzymatic activity of Crystal Structure of Rice BGLU1 E176Q/Y341A Mutant Complexed with Cellotetraose:
3.2.1.21;

Protein crystallography data

The structure of Crystal Structure of Rice BGLU1 E176Q/Y341A Mutant Complexed with Cellotetraose, PDB code: 4qlk was solved by S.Pengthaisong, J.R.Ketudat Cairns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.83
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 63.660, 79.531, 101.989, 90.00, 97.83, 90.00
R / Rfree (%) 15.2 / 16.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Rice BGLU1 E176Q/Y341A Mutant Complexed with Cellotetraose (pdb code 4qlk). 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 Crystal Structure of Rice BGLU1 E176Q/Y341A Mutant Complexed with Cellotetraose, PDB code: 4qlk:

Zinc binding site 1 out of 1 in 4qlk

Go back to Zinc Binding Sites List in 4qlk
Zinc binding site 1 out of 1 in the Crystal Structure of Rice BGLU1 E176Q/Y341A Mutant Complexed with Cellotetraose


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Rice BGLU1 E176Q/Y341A Mutant Complexed with Cellotetraose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1002

b:14.5
occ:1.00
OD2 B:ASP65 2.0 13.5 1.0
ND1 A:HIS68 2.0 15.4 1.0
OD2 A:ASP65 2.0 13.4 1.0
ND1 B:HIS68 2.1 15.0 1.0
CG B:ASP65 2.7 13.3 1.0
CG A:ASP65 2.7 13.3 1.0
OD1 A:ASP65 2.7 13.2 1.0
OD1 B:ASP65 2.8 13.9 1.0
CE1 A:HIS68 2.9 15.8 1.0
CG A:HIS68 3.0 14.8 1.0
CG B:HIS68 3.1 14.9 1.0
CE1 B:HIS68 3.1 15.8 1.0
CB B:HIS68 3.4 15.5 1.0
CB A:HIS68 3.4 15.2 1.0
O B:HOH654 4.0 22.3 1.0
NE2 A:HIS68 4.1 16.1 1.0
CD2 A:HIS68 4.1 15.7 1.0
CB B:ASP65 4.2 12.9 1.0
O A:HOH1120 4.2 20.4 1.0
CB A:ASP65 4.2 12.9 1.0
NE2 B:HIS68 4.2 16.1 1.0
CD2 B:HIS68 4.2 15.8 1.0
O A:HOH1141 4.7 17.9 1.0
CA B:HIS68 4.8 15.9 1.0
CA A:HIS68 4.8 15.4 1.0
O B:HOH667 4.8 17.5 1.0

Reference:

S.Pengthaisong, J.R.Ketudat Cairns. Effects of Active Site Cleft Residues on Oligosaccharide Binding, Hydrolysis, and Glycosynthase Activities of Rice BGLU1 and Its Mutants Protein Sci. V. 23 1738 2014.
ISSN: ISSN 0961-8368
PubMed: 25252199
DOI: 10.1002/PRO.2556
Page generated: Sun Oct 27 06:39:00 2024

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