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Chlorine in PDB 2ype: Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309S, Crystallized with 2',3'- Cyclic Amp

Enzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309S, Crystallized with 2',3'- Cyclic Amp

All present enzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309S, Crystallized with 2',3'- Cyclic Amp:
3.1.4.37;

Protein crystallography data

The structure of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309S, Crystallized with 2',3'- Cyclic Amp, PDB code: 2ype was solved by M.Myllykoski, A.Raasakka, M.Lehtimaki, H.Han, P.Kursula, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 40.800, 47.130, 53.780, 90.00, 94.28, 90.00
R / Rfree (%) 16.7 / 20.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309S, Crystallized with 2',3'- Cyclic Amp (pdb code 2ype). 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 H309S, Crystallized with 2',3'- Cyclic Amp, PDB code: 2ype:

Chlorine binding site 1 out of 1 in 2ype

Go back to Chlorine Binding Sites List in 2ype
Chlorine binding site 1 out of 1 in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309S, Crystallized with 2',3'- Cyclic Amp


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 H309S, Crystallized with 2',3'- Cyclic Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1380

b:59.8
occ:1.00
 O A:HOH2149 2.2 47.7 1.0
HZ3 A:LYS273 2.3 52.2 1.0
HZ1 A:LYS273 2.9 52.2 1.0
NZ A:LYS273 2.9 43.5 1.0
HZ2 A:LYS273 3.1 52.2 1.0
HG23 A:VAL318 3.2 18.3 1.0
O A:ASP317 3.9 20.8 1.0
CG2 A:VAL318 4.0 15.3 1.0
HG21 A:VAL318 4.1 18.3 1.0
HD3 A:LYS273 4.1 34.9 1.0
HA A:VAL318 4.1 23.4 1.0
H1 A:ACY1381 4.2 58.6 1.0
CE A:LYS273 4.2 35.4 1.0
OD2 A:ASP317 4.3 29.1 1.0
OXT A:ACY1381 4.4 58.7 1.0
OD1 A:ASP317 4.4 31.2 1.0
HG2 A:LYS273 4.4 28.6 1.0
CG A:ASP317 4.4 25.2 1.0
HE3 A:LYS273 4.5 42.5 1.0
HG22 A:VAL318 4.6 18.3 1.0
O A:HOH2201 4.6 18.9 1.0
CD A:LYS273 4.6 29.0 1.0
C A:ASP317 4.7 17.1 1.0
C A:ACY1381 4.8 53.3 1.0
CA A:VAL318 4.9 19.5 1.0
O A:HOH2203 4.9 42.8 1.0
HE2 A:LYS273 4.9 42.5 1.0

Reference:

M.Myllykoski, A.Raasakka, M.Lehtimaki, H.Han, I.Kursula, P.Kursula. Crystallographic Analysis of the Reaction Cycle of 2',3'-Cyclic Nucleotide 3'-Phosphodiesterase, A Unique Member of the 2H Phosphoesterase Family J.Mol.Biol. V. 425 4307 2013.
ISSN: ISSN 0022-2836
PubMed: 23831225
DOI: 10.1016/J.JMB.2013.06.012
Page generated: Fri Jul 11 02:45:15 2025

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