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Chlorine in PDB 2yph: Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H230S, Crystallized with 2',3-(Rp)- Cyclic-Amps

Enzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H230S, Crystallized with 2',3-(Rp)- Cyclic-Amps

All present enzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H230S, Crystallized with 2',3-(Rp)- Cyclic-Amps:
3.1.4.37;

Protein crystallography data

The structure of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H230S, Crystallized with 2',3-(Rp)- Cyclic-Amps, PDB code: 2yph 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) 26.89 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.630, 47.530, 107.550, 90.00, 90.00, 90.00
R / Rfree (%) 23 / 28.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H230S, Crystallized with 2',3-(Rp)- Cyclic-Amps (pdb code 2yph). 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 H230S, Crystallized with 2',3-(Rp)- Cyclic-Amps, PDB code: 2yph:

Chlorine binding site 1 out of 1 in 2yph

Go back to Chlorine Binding Sites List in 2yph
Chlorine binding site 1 out of 1 in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H230S, Crystallized with 2',3-(Rp)- Cyclic-Amps


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 H230S, Crystallized with 2',3-(Rp)- Cyclic-Amps within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1380

b:77.5
occ:1.00
 HZ3 A:LYS273 2.5 60.3 1.0
HZ1 A:LYS273 3.0 60.3 1.0
NZ A:LYS273 3.1 50.2 1.0
HG23 A:VAL318 3.3 58.2 1.0
HZ2 A:LYS273 3.3 60.3 1.0
OD2 A:ASP317 3.8 60.0 1.0
O A:ASP317 4.0 51.1 1.0
CG2 A:VAL318 4.1 48.5 1.0
OD1 A:ASP317 4.1 56.3 1.0
HG21 A:VAL318 4.1 58.2 1.0
CG A:ASP317 4.2 57.0 1.0
HG2 A:LYS273 4.3 51.4 1.0
HD3 A:LYS273 4.3 53.0 1.0
CE A:LYS273 4.4 48.4 1.0
HA A:VAL318 4.4 56.9 1.0
O A:HOH2062 4.5 57.1 1.0
HG22 A:VAL318 4.5 58.2 1.0
HE3 A:LYS273 4.7 58.1 1.0
CD A:LYS273 4.8 44.2 1.0
O A:HOH2061 4.8 48.3 1.0
C A:ASP317 4.8 50.2 1.0
O A:HOH2063 5.0 47.4 1.0
O A:HOH2064 5.0 51.0 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 02:45:18 2025

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