Chlorine in PDB 2baj: P38ALPHA Bound to Pyrazolourea

All present enzymatic activity of P38ALPHA Bound to Pyrazolourea:
2.7.1.37;

The structure of P38ALPHA Bound to Pyrazolourea, PDB code: 2baj was solved by S.Gerhardt, R.A.Pauptit, J.Read, J.Breed, R.A.Norman, W.H.Ward, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.25
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.000, 67.104, 87.700, 90.00, 90.00, 90.00
R / Rfree (%)	21.7 / 30.3

The binding sites of Chlorine atom in the P38ALPHA Bound to Pyrazolourea (pdb code 2baj). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the P38ALPHA Bound to Pyrazolourea, PDB code: 2baj:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the P38ALPHA Bound to Pyrazolourea


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of P38ALPHA Bound to Pyrazolourea within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:23.7 occ:1.00 CL1 A:1PP401 0.0 23.7 1.0 C20 A:1PP401 1.8 18.8 1.0 C19 A:1PP401 2.7 19.6 1.0 C21 A:1PP401 2.8 21.6 1.0 N18 A:1PP401 2.9 19.7 1.0 CL2 A:1PP401 3.2 18.7 1.0 CD1 A:LEU75 3.8 23.7 1.0 CB A:LEU104 3.8 20.3 1.0 CD1 A:LEU104 3.9 19.3 1.0 OE2 A:GLU71 3.9 15.6 1.0 CB A:LYS53 4.0 17.3 1.0 C24 A:1PP401 4.0 18.4 1.0 C17 A:1PP401 4.1 19.5 1.0 C22 A:1PP401 4.1 20.1 1.0 CD A:LYS53 4.2 17.0 1.0 CG A:LEU104 4.5 20.3 1.0 C23 A:1PP401 4.5 19.3 1.0 O A:LEU104 4.6 21.6 1.0 N16 A:1PP401 4.7 16.9 1.0 CG A:LYS53 4.8 17.1 1.0 C A:LEU104 4.8 21.3 1.0 CD A:GLU71 4.8 18.1 1.0 O27 A:1PP401 4.8 24.8 1.0 CE A:LYS53 4.9 17.4 1.0 CA A:LEU104 4.9 20.6 1.0 CD1 A:LEU86 5.0 25.1 1.0

Chlorine binding site 2 out of 2 in the P38ALPHA Bound to Pyrazolourea


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of P38ALPHA Bound to Pyrazolourea within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:18.7 occ:1.00 CL2 A:1PP401 0.0 18.7 1.0 C21 A:1PP401 1.8 21.6 1.0 C20 A:1PP401 2.8 18.8 1.0 C22 A:1PP401 2.8 20.1 1.0 CL1 A:1PP401 3.2 23.7 1.0 CG2 A:THR106 3.4 28.1 1.0 O A:LEU104 3.6 21.6 1.0 N A:LYS53 3.6 17.4 1.0 O A:ALA51 3.7 14.6 1.0 C A:ALA51 3.8 16.6 1.0 CB A:ALA51 3.8 17.5 1.0 N A:VAL52 3.9 16.7 1.0 C A:VAL52 3.9 17.1 1.0 CB A:LYS53 4.0 17.3 1.0 CA A:VAL52 4.0 16.5 1.0 C19 A:1PP401 4.1 19.6 1.0 C23 A:1PP401 4.1 19.3 1.0 N A:THR106 4.2 26.2 1.0 CA A:LYS53 4.4 17.8 1.0 C A:LEU104 4.4 21.3 1.0 CA A:ALA51 4.5 17.6 1.0 CB A:THR106 4.5 28.6 1.0 C24 A:1PP401 4.6 18.4 1.0 CG1 A:VAL38 4.7 19.2 1.0 CA A:VAL105 4.7 23.0 1.0 O A:VAL52 4.7 16.5 1.0 C A:VAL105 4.7 24.6 1.0 N A:VAL105 4.9 22.5 1.0

J.E.Sullivan, G.A.Holdgate, D.Campbell, D.Timms, S.Gerhardt, J.Breed, A.L.Breeze, A.Bermingham, R.A.Pauptit, R.A.Norman, K.J.Embrey, J.Read, W.S.Vanscyoc, W.H.Ward. Prevention of MKK6-Dependent Activation By Binding to P38ALPHA Map Kinase Biochemistry V. 44 16475 2005.
ISSN: ISSN 0006-2960
PubMed: 16342939
DOI: 10.1021/BI051714V