Chlorine in PDB 4z84: PKAB3 in Complex with Pyrrolidine Inhibitor 34A

All present enzymatic activity of PKAB3 in Complex with Pyrrolidine Inhibitor 34A:
2.7.11.11;

The structure of PKAB3 in Complex with Pyrrolidine Inhibitor 34A, PDB code: 4z84 was solved by B.A.Lund, K.A.Alam, R.A.Engh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.61 / 1.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.852, 78.431, 79.506, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 23.4

The binding sites of Chlorine atom in the PKAB3 in Complex with Pyrrolidine Inhibitor 34A (pdb code 4z84). 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 PKAB3 in Complex with Pyrrolidine Inhibitor 34A, PDB code: 4z84:

Chlorine binding site 1 out of 1 in the PKAB3 in Complex with Pyrrolidine Inhibitor 34A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of PKAB3 in Complex with Pyrrolidine Inhibitor 34A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:37.3 occ:0.32 CL A:NVX401 0.0 37.3 0.3 CAR A:NVX401 1.7 32.6 1.0 CAE A:NVX401 2.7 33.2 1.0 CAJ A:NVX401 2.7 31.6 1.0 HAE A:NVX401 2.8 39.8 1.0 HAJ A:NVX401 2.8 37.9 1.0 C A:GLY55 2.8 30.8 1.0 HA3 A:GLY52 2.9 44.4 1.0 N A:ARG56 3.1 29.8 1.0 O A:GLY55 3.1 31.3 1.0 HA3 A:GLY55 3.1 39.4 1.0 H A:GLY52 3.2 46.4 1.0 HA A:ARG56 3.3 34.6 1.0 HD22 A:LEU74 3.3 28.9 0.7 CA A:GLY55 3.3 32.8 1.0 H A:ARG56 3.3 35.8 1.0 H A:GLY55 3.4 38.9 1.0 N A:GLY52 3.4 38.7 1.0 HD23 A:LEU74 3.5 28.9 0.7 HD11 A:LEU74 3.5 28.7 0.3 CA A:GLY52 3.5 37.0 1.0 N A:GLY55 3.5 32.4 1.0 HD12 A:LEU74 3.5 28.7 0.3 O A:HOH755 3.5 30.6 1.0 CA A:ARG56 3.6 28.8 1.0 HD13 A:LEU74 3.7 28.7 0.3 HE3 A:LYS72 3.7 37.0 1.0 CD2 A:LEU74 3.7 24.1 0.7 CD1 A:LEU74 3.8 23.9 0.3 HD21 A:LEU74 3.9 28.9 0.7 CAD A:NVX401 4.0 32.8 1.0 CAS A:NVX401 4.0 30.8 1.0 C A:GLY52 4.0 39.3 1.0 H A:PHE54 4.1 47.6 0.9 HG3 A:LYS72 4.1 30.3 1.0 C A:ARG56 4.1 28.0 1.0 HA A:THR51 4.2 47.8 1.0 C A:THR51 4.2 39.1 1.0 HA2 A:GLY55 4.2 39.4 1.0 O A:GLY52 4.3 37.3 1.0 O A:ARG56 4.3 28.0 1.0 HG23 A:VAL57 4.3 29.1 1.0 HA2 A:GLY52 4.3 44.4 1.0 C A:PHE54 4.4 34.9 0.9 CAF A:NVX401 4.5 31.8 1.0 O A:ILE73 4.5 27.2 1.0 CE A:LYS72 4.7 30.8 1.0 N A:SER53 4.7 41.4 0.9 H A:SER53 4.7 49.7 0.9 CA A:THR51 4.8 39.8 1.0 N A:PHE54 4.8 39.7 0.9 HG2 A:LYS72 4.8 30.3 1.0 HAD A:NVX401 4.8 39.3 1.0 CG A:LYS72 4.8 25.3 1.0 HD1 A:PHE54 4.9 47.6 0.9 N A:VAL57 4.9 27.3 1.0 O A:THR51 4.9 40.9 1.0

B.S.Lauber, L.A.Hardegger, A.K.Asraful, B.A.Lund, O.Dumele, M.Harder, B.Kuhn, R.A.Engh, F.Diederich. Addressing the Glycine-Rich Loop of Protein Kinases By A Multi-Facetted Interaction Network: Inhibition of Pka and A Pkb Mimic. Chemistry V. 22 211 2016.
ISSN: ISSN 0947-6539
PubMed: 26578105
DOI: 10.1002/CHEM.201503552