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Chlorine in PDB 6mo6: Crystal Structure of the Selenomethionine-Substituted Human Sulfide:Quinone Oxidoreductase

Protein crystallography data

The structure of Crystal Structure of the Selenomethionine-Substituted Human Sulfide:Quinone Oxidoreductase, PDB code: 6mo6 was solved by M.R.Jackson, M.S.Jorns, P.J.Loll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 62.69 / 2.59
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 119.390, 119.390, 551.858, 90.00, 90.00, 120.00
R / Rfree (%) 18.7 / 24.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Selenomethionine-Substituted Human Sulfide:Quinone Oxidoreductase (pdb code 6mo6). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of the Selenomethionine-Substituted Human Sulfide:Quinone Oxidoreductase, PDB code: 6mo6:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 6mo6

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Chlorine binding site 1 out of 4 in the Crystal Structure of the Selenomethionine-Substituted Human Sulfide:Quinone Oxidoreductase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Selenomethionine-Substituted Human Sulfide:Quinone Oxidoreductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:66.6
occ:1.00
NH1 A:ARG61 3.7 33.6 1.0
NH2 A:ARG61 4.0 35.6 1.0
CA A:GLY436 4.2 35.7 1.0
CZ A:ARG61 4.3 39.8 1.0
N A:GLY436 4.4 39.4 1.0
CA A:GLY354 4.5 37.1 1.0

Chlorine binding site 2 out of 4 in 6mo6

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Chlorine binding site 2 out of 4 in the Crystal Structure of the Selenomethionine-Substituted Human Sulfide:Quinone Oxidoreductase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the Selenomethionine-Substituted Human Sulfide:Quinone Oxidoreductase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl502

b:66.8
occ:1.00
NH2 B:ARG61 3.6 38.4 1.0
NH1 B:ARG61 4.0 24.7 1.0
O B:GLY433 4.1 35.1 1.0
CZ B:ARG61 4.2 36.8 1.0
C B:TYR434 4.2 40.7 1.0
N B:GLY436 4.3 35.5 1.0
N B:TRP435 4.3 42.8 1.0
O B:TYR434 4.5 46.0 1.0
CA B:TYR434 4.5 43.8 1.0
C B:TRP435 4.6 36.5 1.0
CA B:TRP435 4.8 39.5 1.0
CA B:GLY436 4.8 30.0 1.0

Chlorine binding site 3 out of 4 in 6mo6

Go back to Chlorine Binding Sites List in 6mo6
Chlorine binding site 3 out of 4 in the Crystal Structure of the Selenomethionine-Substituted Human Sulfide:Quinone Oxidoreductase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of the Selenomethionine-Substituted Human Sulfide:Quinone Oxidoreductase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl502

b:67.5
occ:1.00
NH1 C:ARG61 3.3 30.0 1.0
NH2 C:ARG61 3.6 35.6 1.0
CZ C:ARG61 3.9 39.4 1.0
N C:GLY436 4.5 27.8 1.0
CA C:GLY436 4.6 31.9 1.0
CA C:GLY354 4.9 35.3 1.0
O C:GLY433 4.9 37.5 1.0
C C:TRP435 5.0 29.1 1.0

Chlorine binding site 4 out of 4 in 6mo6

Go back to Chlorine Binding Sites List in 6mo6
Chlorine binding site 4 out of 4 in the Crystal Structure of the Selenomethionine-Substituted Human Sulfide:Quinone Oxidoreductase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of the Selenomethionine-Substituted Human Sulfide:Quinone Oxidoreductase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl502

b:67.4
occ:1.00
NH1 D:ARG61 3.6 31.6 1.0
NH2 D:ARG61 4.1 36.8 1.0
CZ D:ARG61 4.3 38.7 1.0
N D:GLY436 4.4 29.4 1.0
O D:HOH608 4.5 41.0 1.0
CA D:GLY436 4.6 25.3 1.0
O D:GLY433 4.7 39.7 1.0
C D:TRP435 4.8 31.3 1.0
N D:TRP435 4.9 31.6 1.0

Reference:

M.R.Jackson, P.J.Loll, M.S.Jorns. X-Ray Structure of Human Sulfide:Quinone Oxidoreductase: Insights Into the Mechanism of Mitochondrial Hydrogen Sulfide Oxidation. Structure V. 27 794 2019.
ISSN: ISSN 0969-2126
PubMed: 30905673
DOI: 10.1016/J.STR.2019.03.002
Page generated: Sat Jul 12 16:53:15 2025

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