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Chlorine in PDB 2gtm: Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579

Enzymatic activity of Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579

All present enzymatic activity of Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579:
2.7.11.24;

Protein crystallography data

The structure of Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579, PDB code: 2gtm was solved by R.L.Walter, M.J.Mekel, A.G.Evdokimov, M.E.Pokross, M.Sabat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.80 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.876, 73.627, 76.160, 90.00, 90.00, 90.00
R / Rfree (%) 21.2 / 26.1

Other elements in 2gtm:

The structure of Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579 also contains other interesting chemical elements:

Fluorine (F) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579 (pdb code 2gtm). 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 Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579, PDB code: 2gtm:

Chlorine binding site 1 out of 1 in 2gtm

Go back to Chlorine Binding Sites List in 2gtm
Chlorine binding site 1 out of 1 in the Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl353

b:37.4
occ:1.00
 CL26 A:LID353 0.0 37.4 1.0
C25 A:LID353 1.7 33.7 1.0
C24 A:LID353 2.6 35.9 1.0
C13 A:LID353 2.7 31.9 1.0
N12 A:LID353 2.9 33.2 1.0
C8 A:LID353 3.2 26.4 1.0
N9 A:LID353 3.3 33.6 1.0
CB A:LYS53 3.4 28.9 1.0
N A:LYS53 3.6 26.5 1.0
CB A:ALA51 3.7 29.6 1.0
O A:ALA51 3.8 30.9 1.0
C A:ALA51 3.8 29.0 1.0
C A:VAL52 3.8 29.4 1.0
C21 A:LID353 3.9 34.3 1.0
N A:VAL52 4.0 28.8 1.0
CA A:LYS53 4.0 28.1 1.0
CG1 A:VAL38 4.1 28.8 1.0
C23 A:LID353 4.1 33.4 1.0
N7 A:LID353 4.1 33.6 1.0
O A:LEU104 4.1 23.6 1.0
CA A:VAL52 4.2 29.6 1.0
CG2 A:THR106 4.3 37.0 1.0
C2 A:LID353 4.3 28.3 1.0
O A:VAL52 4.3 25.4 1.0
CG2 A:VAL38 4.3 31.9 1.0
CA A:ALA51 4.4 31.0 1.0
C22 A:LID353 4.5 35.3 1.0
CG A:LYS53 4.6 29.5 1.0
C3 A:LID353 4.6 28.0 1.0
CD A:LYS53 4.6 37.9 1.0
CB A:VAL38 4.8 30.3 1.0
N A:THR106 4.9 30.7 1.0
C10 A:LID353 4.9 34.5 1.0
CB A:THR106 5.0 33.0 1.0

Reference:

M.Sabat, J.C.Vanrens, M.P.Clark, T.A.Brugel, J.Maier, R.G.Bookland, M.J.Laufersweiler, S.K.Laughlin, A.Golebiowski, B.De, L.C.Hsieh, R.L.Walter, M.J.Mekel, M.J.Janusz. The Development of Novel C-2, C-8, and N-9 Trisubstituted Purines As Inhibitors of Tnf-Alpha Production. Bioorg.Med.Chem.Lett. V. 16 4360 2006.
ISSN: ISSN 0960-894X
PubMed: 16750367
DOI: 10.1016/J.BMCL.2006.05.050
Page generated: Sat Jul 20 07:39:26 2024

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