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Chlorine in PDB 5klv: Structure of Bos Taurus Cytochrome BC1 with Fenamidone Inhibited

Enzymatic activity of Structure of Bos Taurus Cytochrome BC1 with Fenamidone Inhibited

All present enzymatic activity of Structure of Bos Taurus Cytochrome BC1 with Fenamidone Inhibited:
1.10.2.2;

Protein crystallography data

The structure of Structure of Bos Taurus Cytochrome BC1 with Fenamidone Inhibited, PDB code: 5klv was solved by D.Xia, L.Esser, F.Zhou, Y.Zhou, Y.Xiao, W.K.Tang, C.A.Yu, Z.Qin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.68 / 2.65
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 153.986, 153.986, 592.713, 90.00, 90.00, 90.00
R / Rfree (%) 22.8 / 26.9

Other elements in 5klv:

The structure of Structure of Bos Taurus Cytochrome BC1 with Fenamidone Inhibited also contains other interesting chemical elements:

Iron (Fe) 5 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Bos Taurus Cytochrome BC1 with Fenamidone Inhibited (pdb code 5klv). 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 Structure of Bos Taurus Cytochrome BC1 with Fenamidone Inhibited, PDB code: 5klv:

Chlorine binding site 1 out of 1 in 5klv

Go back to Chlorine Binding Sites List in 5klv
Chlorine binding site 1 out of 1 in the Structure of Bos Taurus Cytochrome BC1 with Fenamidone Inhibited


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Bos Taurus Cytochrome BC1 with Fenamidone Inhibited within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl1005

b:62.3
occ:1.00
HH22 C:ARG80 3.3 0.9 1.0
HH12 C:ARG80 3.6 0.5 1.0
HE2 C:TYR256 3.7 0.7 1.0
HG12 C:VAL66 3.8 94.4 1.0
CE2 C:TYR256 3.8 93.7 1.0
HD2 C:TYR256 3.8 0.7 1.0
NH2 C:ARG80 3.8 99.7 1.0
CD2 C:TYR256 3.9 93.7 1.0
HG11 C:VAL66 4.0 94.4 1.0
HA C:TYR256 4.1 0.7 1.0
NH1 C:ARG80 4.1 0.0 1.0
HB C:VAL66 4.2 95.9 1.0
CG1 C:VAL66 4.3 78.5 1.0
HZ C:PHE63 4.3 0.4 1.0
CZ C:ARG80 4.3 99.0 1.0
CZ C:PHE63 4.3 93.5 1.0
HH21 C:ARG80 4.3 0.9 1.0
OG1 C:THR67 4.4 85.4 1.0
CZ C:TYR256 4.5 92.5 1.0
CE1 C:PHE63 4.5 92.0 1.0
HE1 C:PHE63 4.6 0.6 1.0
CG C:TYR256 4.7 92.6 1.0
CZ D:TYR115 4.7 0.2 1.0
OH D:TYR115 4.7 0.7 1.0
HA C:THR67 4.7 0.1 1.0
HH11 C:ARG80 4.8 0.5 1.0
CE2 C:PHE63 4.8 94.4 1.0
CB C:VAL66 4.8 79.7 1.0
HH C:TYR256 4.8 0.4 1.0
HG1 C:THR67 4.8 0.7 1.0
H C:THR67 4.8 99.3 1.0
HH D:TYR115 4.8 0.1 1.0
N C:THR67 4.9 82.6 1.0
CE1 D:TYR115 5.0 0.0 1.0
O C:ASN255 5.0 87.4 1.0
O C:PHE63 5.0 89.0 1.0
CE2 D:TYR115 5.0 0.8 1.0

Reference:

L.Esser, F.Zhou, Y.Zhou, Y.Xiao, W.K.Tang, C.A.Yu, Z.Qin, D.Xia. Hydrogen Bonding to the Substrate Is Not Required For Rieske Iron-Sulfur Protein Docking to the Quinol Oxidation Site of Complex III. J.Biol.Chem. V. 291 25019 2016.
ISSN: ESSN 1083-351X
PubMed: 27758861
DOI: 10.1074/JBC.M116.744391
Page generated: Sat Dec 12 11:56:49 2020

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