Atomistry » Chlorine » PDB 4k2a-4kb9 » 4k8h
Atomistry »
  Chlorine »
    PDB 4k2a-4kb9 »
      4k8h »

Chlorine in PDB 4k8h: OYE1-W116V Complexed with (R)-Carvone

Enzymatic activity of OYE1-W116V Complexed with (R)-Carvone

All present enzymatic activity of OYE1-W116V Complexed with (R)-Carvone:
1.6.99.1;

Protein crystallography data

The structure of OYE1-W116V Complexed with (R)-Carvone, PDB code: 4k8h was solved by B.Sullivan, 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) 35.48 / 1.55
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 141.443, 141.443, 42.851, 90.00, 90.00, 90.00
R / Rfree (%) 12.4 / 16.2

Other elements in 4k8h:

The structure of OYE1-W116V Complexed with (R)-Carvone also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the OYE1-W116V Complexed with (R)-Carvone (pdb code 4k8h). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the OYE1-W116V Complexed with (R)-Carvone, PDB code: 4k8h:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 4k8h

Go back to Chlorine Binding Sites List in 4k8h
Chlorine binding site 1 out of 2 in the OYE1-W116V Complexed with (R)-Carvone


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of OYE1-W116V Complexed with (R)-Carvone within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:23.2
occ:1.00
H A:ASP83 2.4 16.5 1.0
HD22 A:ASN126 2.4 22.4 1.0
HA A:TYR82 3.0 13.6 1.0
HD2 A:PHE123 3.0 22.9 1.0
ND2 A:ASN126 3.2 18.7 1.0
O A:HOH569 3.2 17.7 1.0
N A:ASP83 3.2 13.7 1.0
HE2 A:PHE123 3.3 27.3 1.0
HB2 A:ASP83 3.3 21.7 1.0
HD21 A:ASN126 3.3 22.4 1.0
CD2 A:PHE123 3.8 19.1 1.0
CA A:TYR82 3.8 11.3 1.0
CE2 A:PHE123 3.9 22.8 1.0
CB A:ASP83 4.0 18.1 1.0
C A:TYR82 4.0 13.9 1.0
HB3 A:TYR82 4.1 14.7 1.0
CA A:ASP83 4.2 14.5 1.0
CG A:ASP83 4.2 19.7 1.0
HD1 A:TYR82 4.2 15.0 1.0
H A:ASN84 4.2 14.2 1.0
CG A:ASN126 4.3 20.2 1.0
O A:HOH608 4.3 26.9 1.0
OD2 A:ASP83 4.4 20.4 1.0
O A:GLY81 4.4 14.7 1.0
CB A:TYR82 4.5 12.2 1.0
OD1 A:ASN126 4.7 21.5 1.0
C23 A:1PE408 4.7 21.5 0.7
OD1 A:ASP83 4.8 21.4 1.0
HB3 A:ASP83 4.8 21.7 1.0
N A:ASN84 4.9 11.8 1.0
HA A:ASP83 4.9 17.4 1.0
CD1 A:TYR82 4.9 12.5 1.0
N A:TYR82 4.9 12.6 1.0
OD1 A:ASN84 5.0 16.5 1.0

Chlorine binding site 2 out of 2 in 4k8h

Go back to Chlorine Binding Sites List in 4k8h
Chlorine binding site 2 out of 2 in the OYE1-W116V Complexed with (R)-Carvone


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of OYE1-W116V Complexed with (R)-Carvone within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl403

b:51.1
occ:1.00
O A:HOH980 3.6 37.8 1.0
HB2 A:TYR313 3.6 13.1 1.0
HB3 A:ASP310 3.6 15.4 1.0
HH21 A:ARG322 3.7 17.2 0.6
HH22 A:ARG322 3.8 17.2 0.6
O A:HOH724 3.9 32.7 1.0
CG A:TYR313 3.9 11.1 1.0
CG A:ASP310 4.0 13.9 1.0
HA A:ASP310 4.0 12.2 1.0
NH2 A:ARG322 4.1 14.3 0.6
CB A:TYR313 4.1 10.9 1.0
OD1 A:ASP310 4.1 17.2 1.0
CD1 A:TYR313 4.1 11.4 1.0
HB3 A:TYR313 4.1 13.1 1.0
HH12 A:ARG322 4.1 17.1 0.4
CB A:ASP310 4.2 12.8 1.0
HD1 A:TYR313 4.3 13.6 1.0
CD2 A:TYR313 4.3 11.6 1.0
OD2 A:ASP310 4.4 18.7 1.0
O A:ASP310 4.5 12.5 1.0
CA A:ASP310 4.6 10.1 1.0
HD2 A:TYR313 4.6 14.0 1.0
O A:HOH920 4.6 23.1 1.0
CE1 A:TYR313 4.6 12.7 1.0
NH1 A:ARG322 4.8 14.2 0.4
CE2 A:TYR313 4.8 12.2 1.0
HB2 A:ASP339 4.9 15.3 1.0
HH11 A:ARG322 5.0 17.1 0.4
CZ A:TYR313 5.0 11.8 1.0
O A:HOH952 5.0 35.9 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: Sat Dec 12 10:50:05 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy