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Chlorine in PDB 4ct1: Human PDK1-Pkczeta Kinase Chimera in Complex with Allosteric Compound PS315 Bound to the Pif-Pocket

Enzymatic activity of Human PDK1-Pkczeta Kinase Chimera in Complex with Allosteric Compound PS315 Bound to the Pif-Pocket

All present enzymatic activity of Human PDK1-Pkczeta Kinase Chimera in Complex with Allosteric Compound PS315 Bound to the Pif-Pocket:
2.7.11.1;

Protein crystallography data

The structure of Human PDK1-Pkczeta Kinase Chimera in Complex with Allosteric Compound PS315 Bound to the Pif-Pocket, PDB code: 4ct1 was solved by J.O.Schulze, H.Zhang, L.A.Lopez-Garcia, R.M.Biondi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.263 / 1.85
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 148.600, 44.610, 48.000, 90.00, 101.84, 90.00
R / Rfree (%) 16.99 / 21.55

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Human PDK1-Pkczeta Kinase Chimera in Complex with Allosteric Compound PS315 Bound to the Pif-Pocket (pdb code 4ct1). 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 Human PDK1-Pkczeta Kinase Chimera in Complex with Allosteric Compound PS315 Bound to the Pif-Pocket, PDB code: 4ct1:

Chlorine binding site 1 out of 1 in 4ct1

Go back to Chlorine Binding Sites List in 4ct1
Chlorine binding site 1 out of 1 in the Human PDK1-Pkczeta Kinase Chimera in Complex with Allosteric Compound PS315 Bound to the Pif-Pocket


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human PDK1-Pkczeta Kinase Chimera in Complex with Allosteric Compound PS315 Bound to the Pif-Pocket within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl600

b:87.3
occ:1.00
 CL7 A:31S600 0.0 87.3 1.0
C5 A:31S600 1.8 79.5 1.0
C4 A:31S600 2.8 79.4 1.0
C6 A:31S600 2.8 79.7 1.0
H6 A:31S600 2.9 95.7 1.0
H4 A:31S600 2.9 95.2 1.0
HG12 A:ILE124 3.3 47.8 1.0
HG2 A:LYS115 3.5 40.2 1.0
HD12 A:ILE124 3.6 51.9 1.0
HD11 A:ILE124 3.7 51.9 1.0
HD12 A:LEU155 3.8 35.4 1.0
CD1 A:ILE124 3.9 43.2 1.0
HG21 A:VAL118 4.0 50.4 1.0
CG1 A:ILE124 4.1 39.9 1.0
C3 A:31S600 4.1 79.4 1.0
C1 A:31S600 4.1 79.6 1.0
HG22 A:VAL118 4.2 50.4 1.0
HE2 A:LYS115 4.3 40.0 1.0
HG21 A:ILE124 4.3 44.7 1.0
HD22 A:LEU155 4.4 34.9 1.0
CG A:LYS115 4.5 33.5 1.0
HB3 A:LYS115 4.5 41.4 1.0
CG2 A:VAL118 4.6 42.0 1.0
HA A:LYS115 4.6 40.7 1.0
HG13 A:ILE124 4.6 47.8 1.0
C2 A:31S600 4.6 79.1 1.0
HG22 A:ILE124 4.7 44.7 1.0
CD1 A:LEU155 4.7 29.5 1.0
CG2 A:ILE124 4.9 37.2 1.0
HD13 A:ILE124 4.9 51.9 1.0
CB A:LYS115 4.9 34.5 1.0
H3 A:31S600 4.9 95.3 1.0
H1 A:31S600 4.9 95.5 1.0
HD3 A:LYS115 4.9 42.0 1.0

Reference:

H.Zhang, S.Neimanis, L.A.Lopez-Garcia, J.M.Arencibia, S.Amon, A.Stroba, S.Zeuzem, E.Proschak, H.Stark, A.F.Bauer, K.Busschots, T.J.Jorgensen, M.Engel, J.O.Schulze, R.M.Biondi. Molecular Mechanism of Regulation of the Atypical Protein Kinase C By N-Terminal Domains and An Allosteric Small Compound. Chem.Biol. V. 21 754 2014.
ISSN: ISSN 1074-5521
PubMed: 24836908
DOI: 10.1016/J.CHEMBIOL.2014.04.007
Page generated: Sun Jul 21 11:32:51 2024

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