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Chlorine in PDB 2wkt: Biosynthetic Thiolase From Z. Ramigera. Complex of the N316A Mutant with Coenzyme A.

Enzymatic activity of Biosynthetic Thiolase From Z. Ramigera. Complex of the N316A Mutant with Coenzyme A.

All present enzymatic activity of Biosynthetic Thiolase From Z. Ramigera. Complex of the N316A Mutant with Coenzyme A.:
2.3.1.9;

Protein crystallography data

The structure of Biosynthetic Thiolase From Z. Ramigera. Complex of the N316A Mutant with Coenzyme A., PDB code: 2wkt 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) 19.626 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 84.600, 79.200, 148.700, 90.00, 92.80, 90.00
R / Rfree (%) 18.66 / 23.56

Other elements in 2wkt:

The structure of Biosynthetic Thiolase From Z. Ramigera. Complex of the N316A Mutant with Coenzyme A. also contains other interesting chemical elements:

Potassium (K) 1 atom
Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Biosynthetic Thiolase From Z. Ramigera. Complex of the N316A Mutant with Coenzyme A. (pdb code 2wkt). 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 N316A Mutant with Coenzyme A., PDB code: 2wkt:

Chlorine binding site 1 out of 1 in 2wkt

Go back to Chlorine Binding Sites List in 2wkt
Chlorine binding site 1 out of 1 in the Biosynthetic Thiolase From Z. Ramigera. Complex of the N316A Mutant with Coenzyme A.


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 N316A Mutant with Coenzyme A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1396

b:0.9
occ:1.00
 O A:MET85 2.4 9.7 1.0
N A:MET85 2.5 7.6 1.0
N A:GLN56 2.6 5.6 1.0
O A:LEU54 2.6 11.1 1.0
C A:MET85 3.1 5.7 1.0
C A:GLY55 3.1 3.1 1.0
C A:GLY84 3.2 3.7 1.0
CA A:GLY84 3.3 7.4 1.0
O A:GLN56 3.3 7.2 1.0
CA A:GLY55 3.3 0.7 1.0
CA A:MET85 3.3 4.7 1.0
CA A:GLN56 3.4 0.9 1.0
CB A:GLN56 3.4 2.0 1.0
K A:K1395 3.4 43.9 1.0
C A:LEU54 3.6 9.6 1.0
O A:HOH2082 3.6 9.5 1.0
C A:GLN56 3.7 5.5 1.0
N A:GLY55 3.9 5.9 1.0
O A:GLY55 4.1 10.4 1.0
O A:GLY84 4.2 5.6 1.0
N A:ASN86 4.3 0.8 1.0
O B:HOH2127 4.3 9.0 1.0
CB A:MET85 4.6 0.7 1.0
CG A:MET85 4.7 9.4 1.0
N A:GLY84 4.7 11.5 1.0
CG A:GLN56 4.8 1.0 1.0
CA A:ASN86 4.8 5.3 1.0
OE1 A:GLN56 5.0 12.2 1.0
CA A:LEU54 5.0 2.5 1.0
CB A:ASN86 5.0 8.0 1.0

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 Jul 20 13:00:24 2024

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