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Chlorine in PDB 4h6k: W116I Mutant of OYE1

Enzymatic activity of W116I Mutant of OYE1

All present enzymatic activity of W116I Mutant of OYE1:
1.6.99.1;

Protein crystallography data

The structure of W116I Mutant of OYE1, PDB code: 4h6k was solved by Y.A.Pompeu, J.D.Stewart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.51 / 1.55
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 140.930, 140.930, 42.460, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 20.4

Other elements in 4h6k:

The structure of W116I Mutant of OYE1 also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the W116I Mutant of OYE1 (pdb code 4h6k). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the W116I Mutant of OYE1, PDB code: 4h6k:

Chlorine binding site 1 out of 1 in 4h6k

Go back to Chlorine Binding Sites List in 4h6k
Chlorine binding site 1 out of 1 in the W116I Mutant of OYE1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of W116I Mutant of OYE1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:37.5
occ:1.00
N A:ASP83 3.2 22.2 1.0
O A:HOH525 3.2 29.3 1.0
ND2 A:ASN126 3.2 31.5 1.0
O A:HOH622 3.5 53.2 1.0
CB A:ASP83 3.8 23.4 1.0
CD2 A:PHE123 3.8 32.6 1.0
CE2 A:PHE123 3.9 32.8 1.0
CA A:TYR82 4.0 22.6 1.0
C A:TYR82 4.1 24.6 1.0
CA A:ASP83 4.1 26.4 1.0
CG A:ASP83 4.1 34.7 1.0
OD2 A:ASP83 4.3 37.0 1.0
CG A:ASN126 4.4 35.7 1.0
O A:GLY81 4.5 26.5 1.0
O A:HOH795 4.6 43.8 1.0
CB A:TYR82 4.7 24.6 1.0
OD1 A:ASP83 4.7 31.9 1.0
OD1 A:ASN126 4.7 37.7 1.0
N A:ASN84 4.7 22.7 1.0
OD1 A:ASN84 4.8 29.4 1.0
C A:ASP83 5.0 22.3 1.0

Reference:

Y.A.Pompeu, B.Sullivan, J.D.Stewart. X‑Ray Crystallography Reveals How Subtle Changes Control the Orientation of Substrate Binding in An Alkene Reductase Acs Catalysis V. 3 2376 2013.
ISSN: ESSN 2155-5435
DOI: 10.1021/CS400622E
Page generated: Fri Jul 11 16:09:43 2025

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