Chlorine in PDB 5jhb: Structure of Phosphoinositide 3-Kinase Gamma (PI3K) Bound to the Potent Inhibitor PIKIN3

Enzymatic activity of Structure of Phosphoinositide 3-Kinase Gamma (PI3K) Bound to the Potent Inhibitor PIKIN3

All present enzymatic activity of Structure of Phosphoinositide 3-Kinase Gamma (PI3K) Bound to the Potent Inhibitor PIKIN3:
2.7.1.153; 2.7.11.1;

Protein crystallography data

The structure of Structure of Phosphoinositide 3-Kinase Gamma (PI3K) Bound to the Potent Inhibitor PIKIN3, PDB code: 5jhb was solved by J.E.Burke, A.J.Inglis, R.L.Williams, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	62.08 / 2.48
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	142.530, 67.600, 106.550, 90.00, 96.23, 90.00
*R / R_free (%)*	23.1 / 27.7

Other elements in 5jhb:

The structure of Structure of Phosphoinositide 3-Kinase Gamma (PI3K) Bound to the Potent Inhibitor PIKIN3 also contains other interesting chemical elements:

Fluorine

(F)

3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Phosphoinositide 3-Kinase Gamma (PI3K) Bound to the Potent Inhibitor PIKIN3 (pdb code 5jhb). 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 Structure of Phosphoinositide 3-Kinase Gamma (PI3K) Bound to the Potent Inhibitor PIKIN3, PDB code: 5jhb:

Chlorine binding site 1 out of 1 in 5jhb

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Chlorine Binding Sites List in 5jhb

Chlorine binding site 1 out of 1 in the Structure of Phosphoinositide 3-Kinase Gamma (PI3K) Bound to the Potent Inhibitor PIKIN3

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Phosphoinositide 3-Kinase Gamma (PI3K) Bound to the Potent Inhibitor PIKIN3 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl1201 b:0.7 occ:1.00	CL	A:6K51201	0.0	0.7	1.0
	CBD	A:6K51201	1.9	0.6	1.0
	HBD1	A:6K51201	2.4	0.9	1.0
	HBD2	A:6K51201	2.4	0.9	1.0
	HAZ1	A:6K51201	2.5	92.9	1.0
	CBA	A:6K51201	2.9	98.2	1.0
	CAZ	A:6K51201	3.1	77.4	1.0
	O	A:HOH1310	3.2	81.5	1.0
	HAV2	A:6K51201	3.8	0.8	1.0
	CAV	A:6K51201	3.9	84.0	1.0
	HAZ2	A:6K51201	3.9	92.9	1.0
	NAU	A:6K51201	4.1	79.8	1.0
	CBB	A:6K51201	4.1	0.1	1.0
	OBC	A:6K51201	4.2	0.6	1.0
	CE	A:MET953	4.4	57.6	1.0
	CZ3	A:TRP812	4.5	75.7	1.0
	HBB1	A:6K51201	4.5	0.7	1.0
	HAW2	A:6K51201	4.7	83.9	1.0
	HBC1	A:6K51201	4.7	0.7	1.0
	O	A:ALA885	4.8	68.8	1.0
	HAV1	A:6K51201	4.8	0.8	1.0
	CH2	A:TRP812	4.9	68.7	1.0

Reference:

T.Bohnacker, A.E.Prota, F.Beaufils, J.E.Burke, A.Melone, A.J.Inglis, D.Rageot, A.M.Sele, V.Cmiljanovic, N.Cmiljanovic, K.Bargsten, A.Aher, A.Akhmanova, J.F.Diaz, D.Fabbro, M.Zvelebil, R.L.Williams, M.O.Steinmetz, M.P.Wymann. Deconvolution of Buparlisib'S Mechanism of Action Defines Specific PI3K and Tubulin Inhibitors For Therapeutic Intervention. Nat Commun V. 8 14683 2017.
ISSN: ESSN 2041-1723
PubMed: 28276440
DOI: 10.1038/NCOMMS14683

Page generated: Sat Jul 12 03:38:08 2025

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