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Chlorine in PDB 2wl5: Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A.
Enzymatic activity of Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A.
All present enzymatic activity of Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A.:
2.3.1.9;
2.3.1.9;
Protein crystallography data
The structure of Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A., PDB code: 2wl5
was solved by
G.Merilainen,
V.Poikela,
P.Kursula,
R.K.Wierenga,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 19.39 / 1.80 |
| Space group | P 1 21 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 84.700, 79.200, 153.000, 90.00, 92.50, 90.00 |
| R / Rfree (%) | 22.1 / 25.7 |
Other elements in 2wl5:
The structure of Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A. also contains other interesting chemical elements:
| Sodium | (Na) | 1 atom |
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A.
(pdb code 2wl5). 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 Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A., PDB code: 2wl5:
In total only one binding site of Chlorine was determined in the Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A., PDB code: 2wl5:
Chlorine binding site 1 out of 1 in 2wl5
Go back to
Chlorine Binding Sites List in 2wl5
Chlorine binding site 1 out
of 1 in the Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A.
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 Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A. within 5.0Å range: |
Reference:
G.Merilainen,
V.Poikela,
P.Kursula,
R.K.Wierenga.
The Thiolase Reaction Mechanism: the Importance of ASN316 and HIS348 For Stabilizing the Enolate Intermediate of the Claisen Condensation. Biochemistry V. 48 11011 2009.
ISSN: ISSN 0006-2960
PubMed: 19842716
DOI: 10.1021/BI901069H
Page generated: Sat Dec 12 09:23:38 2020
ISSN: ISSN 0006-2960
PubMed: 19842716
DOI: 10.1021/BI901069H
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