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Chlorine in PDB 7o5m: Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Synechocystis Sp. Pcc 6803 Cocrystallized with Adenosine in the Presence of Na+ Cations
Enzymatic activity of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Synechocystis Sp. Pcc 6803 Cocrystallized with Adenosine in the Presence of Na+ Cations
All present enzymatic activity of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Synechocystis Sp. Pcc 6803 Cocrystallized with Adenosine in the Presence of Na+ Cations:
3.3.1.1;
3.3.1.1;
Protein crystallography data
The structure of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Synechocystis Sp. Pcc 6803 Cocrystallized with Adenosine in the Presence of Na+ Cations, PDB code: 7o5m
was solved by
P.H.Malecki,
B.Imiolczyk,
J.Barciszewski,
J.Czyrko-Horczak,
K.Brzezinski,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 42.27 / 2.20 |
| Space group | C 2 2 21 |
| Cell size a, b, c (Å), α, β, γ (°) | 120.77, 197.13, 82.23, 90, 90, 90 |
| R / Rfree (%) | 19.2 / 24.9 |
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Synechocystis Sp. Pcc 6803 Cocrystallized with Adenosine in the Presence of Na+ Cations
(pdb code 7o5m). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Synechocystis Sp. Pcc 6803 Cocrystallized with Adenosine in the Presence of Na+ Cations, PDB code: 7o5m:
Jump to Chlorine binding site number: 1; 2; 3;
In total 3 binding sites of Chlorine where determined in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Synechocystis Sp. Pcc 6803 Cocrystallized with Adenosine in the Presence of Na+ Cations, PDB code: 7o5m:
Jump to Chlorine binding site number: 1; 2; 3;
Chlorine binding site 1 out of 3 in 7o5m
Go back to
Chlorine Binding Sites List in 7o5m
Chlorine binding site 1 out
of 3 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Synechocystis Sp. Pcc 6803 Cocrystallized with Adenosine in the Presence of Na+ Cations
Mono view
Stereo pair view
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 S-Adenosyl-L-Homocysteine Hydrolase From Synechocystis Sp. Pcc 6803 Cocrystallized with Adenosine in the Presence of Na+ Cations within 5.0Å range:
|
Chlorine binding site 2 out of 3 in 7o5m
Go back to
Chlorine Binding Sites List in 7o5m
Chlorine binding site 2 out
of 3 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Synechocystis Sp. Pcc 6803 Cocrystallized with Adenosine in the Presence of Na+ Cations
Mono view
Stereo pair view
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 S-Adenosyl-L-Homocysteine Hydrolase From Synechocystis Sp. Pcc 6803 Cocrystallized with Adenosine in the Presence of Na+ Cations within 5.0Å range:
|
Chlorine binding site 3 out of 3 in 7o5m
Go back to
Chlorine Binding Sites List in 7o5m
Chlorine binding site 3 out
of 3 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Synechocystis Sp. Pcc 6803 Cocrystallized with Adenosine in the Presence of Na+ Cations
Mono view
Stereo pair view
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 S-Adenosyl-L-Homocysteine Hydrolase From Synechocystis Sp. Pcc 6803 Cocrystallized with Adenosine in the Presence of Na+ Cations within 5.0Å range:
|
Reference:
P.H.Malecki,
B.Imiolczyk,
J.Barciszewski,
J.Czyrko-Horczak,
J.Sliwiak,
M.Gawel,
K.Wozniak,
M.Jaskolski,
K.Brzezinski.
Biochemical and Structural Insights Into An Unusual, Alkali-Metal-Independent S-Adenosyl-L-Homocysteine Hydrolase From Synechocystis Sp. Pcc 6803. Acta Crystallogr D Struct V. 78 865 2022BIOL.
ISSN: ISSN 2059-7983
PubMed: 35775986
DOI: 10.1107/S2059798322005605
Page generated: Sun Jul 13 04:43:08 2025
ISSN: ISSN 2059-7983
PubMed: 35775986
DOI: 10.1107/S2059798322005605
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