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Chlorine in PDB 4wex: Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation Y168S

Enzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation Y168S

All present enzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation Y168S:
3.1.4.37;

Protein crystallography data

The structure of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation Y168S, PDB code: 4wex was solved by M.Myllykoski, A.Raasakka, P.Kursula, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.97 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 38.170, 48.240, 51.220, 90.00, 95.62, 90.00
R / Rfree (%) 19.9 / 23.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation Y168S (pdb code 4wex). 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 Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation Y168S, PDB code: 4wex:

Chlorine binding site 1 out of 1 in 4wex

Go back to Chlorine Binding Sites List in 4wex
Chlorine binding site 1 out of 1 in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation Y168S


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation Y168S within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl401

b:44.1
occ:1.00
 HG A:SER297 2.1 60.7 1.0
HE1 A:TRP289 2.4 37.8 1.0
H A:SER297 2.5 52.5 1.0
H A:GLY305 2.7 36.1 1.0
OG A:SER297 2.9 50.6 1.0
HG2 A:ARG307 3.0 55.6 1.0
HD12 A:LEU293 3.2 56.5 1.0
NE1 A:TRP289 3.2 31.5 1.0
HD3 A:ARG307 3.2 55.3 1.0
N A:SER297 3.3 43.8 1.0
HA A:PRO304 3.4 63.6 1.0
HB2 A:SER297 3.5 58.5 1.0
N A:GLY305 3.5 30.1 1.0
HA A:PRO296 3.6 53.3 1.0
CB A:SER297 3.6 48.8 1.0
CG A:ARG307 3.8 46.4 1.0
CD A:ARG307 3.9 46.1 1.0
HD1 A:TRP289 3.9 36.1 1.0
CD1 A:TRP289 4.0 30.1 1.0
HB2 A:PRO296 4.0 54.7 1.0
HG3 A:ARG307 4.0 55.6 1.0
O A:HOH523 4.0 35.1 1.0
H A:ARG307 4.0 40.8 1.0
CA A:SER297 4.1 44.7 1.0
CD1 A:LEU293 4.1 47.1 1.0
HA2 A:GLY305 4.1 28.5 1.0
H A:SER306 4.1 35.1 1.0
CA A:PRO296 4.2 44.5 1.0
HZ2 A:TRP289 4.2 37.8 1.0
CA A:PRO304 4.2 53.0 1.0
CE2 A:TRP289 4.2 31.1 1.0
C A:PRO296 4.2 45.9 1.0
HD2 A:ARG307 4.3 55.3 1.0
HB3 A:PRO296 4.3 54.7 1.0
HB2 A:LEU293 4.3 55.0 1.0
CA A:GLY305 4.3 23.7 1.0
C A:PRO304 4.4 38.9 1.0
CB A:PRO296 4.4 45.6 1.0
HD13 A:LEU293 4.4 56.5 1.0
HD11 A:LEU293 4.5 56.5 1.0
HB3 A:SER297 4.5 58.5 1.0
HB3 A:PRO304 4.5 74.6 1.0
CZ2 A:TRP289 4.6 31.5 1.0
HA A:SER297 4.6 53.6 1.0
N A:SER306 4.6 29.3 1.0
H A:ALA298 4.7 44.1 1.0
C A:GLY305 4.9 26.9 1.0
N A:ARG307 4.9 34.0 1.0
CB A:PRO304 5.0 62.2 1.0

Reference:

A.Raasakka, M.Myllykoski, S.Laulumaa, M.Lehtimaki, M.Hartlein, M.Moulin, I.Kursula, P.Kursula. Determinants of Ligand Binding and Catalytic Activity in the Myelin Enzyme 2',3'-Cyclic Nucleotide 3'-Phosphodiesterase. Sci Rep V. 5 16520 2015.
ISSN: ESSN 2045-2322
PubMed: 26563764
DOI: 10.1038/SREP16520
Page generated: Fri Jul 26 02:52:48 2024

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