Fluorine in PDB 5orw: Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment

Enzymatic activity of Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment

All present enzymatic activity of Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment:
2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment, PDB code: 5orw was solved by P.J.Mcintyre, P.M.Collins, F.Von Delft, R.Bayliss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	55.40 / 2.00
*Space group*	P 6₁ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	82.510, 82.510, 175.390, 90.00, 90.00, 120.00
*R / R_free (%)*	21.5 / 27

Other elements in 5orw:

The structure of Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment (pdb code 5orw). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment, PDB code: 5orw:

Fluorine binding site 1 out of 1 in 5orw

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Fluorine Binding Sites List in 5orw

Fluorine binding site 1 out of 1 in the Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment

Mono view

Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:F404 b:76.8 occ:1.00	F	A:A6E404	0.0	76.8	1.0
	C	A:A6E404	1.3	75.5	1.0
	C12	A:A6E404	2.3	73.9	1.0
	C1	A:A6E404	2.3	73.7	1.0
	CG	A:ARG179	3.6	67.6	1.0
	C11	A:A6E404	3.6	79.9	1.0
	C2	A:A6E404	3.6	78.7	1.0
	CA	A:ARG179	3.6	49.7	1.0
	CB	A:VAL182	3.8	52.1	1.0
	CG2	A:VAL182	3.8	50.5	1.0
	C3	A:A6E404	4.1	80.7	1.0
	CB	A:ARG179	4.2	52.3	1.0
	CG1	A:VAL182	4.2	50.5	1.0
	N	A:ARG179	4.3	49.1	1.0
	O	A:ARG179	4.3	47.9	1.0
	O	A:LEU178	4.5	45.7	1.0
	C	A:ARG179	4.5	49.2	1.0
	CZ	A:TYR199	4.5	72.2	1.0
	CE1	A:TYR199	4.7	67.9	1.0
	C	A:LEU178	4.7	51.8	1.0
	OH	A:TYR199	4.7	73.7	1.0
	CD	A:ARG179	4.8	64.3	1.0
	CE2	A:TYR199	4.8	71.7	1.0
	NE	A:ARG179	4.9	69.2	1.0

Reference:

P.J.Mcintyre, P.M.Collins, L.Vrzal, K.Birchall, L.H.Arnold, C.Mpamhanga, P.J.Coombs, S.G.Burgess, M.W.Richards, A.Winter, V.Veverka, F.V.Delft, A.Merritt, R.Bayliss. Characterization of Three Druggable Hot-Spots in the Aurora-A/TPX2 Interaction Using Biochemical, Biophysical, and Fragment-Based Approaches. Acs Chem. Biol. V. 12 2906 2017.
ISSN: ESSN 1554-8937
PubMed: 29045126
DOI: 10.1021/ACSCHEMBIO.7B00537

Page generated: Thu Aug 1 12:33:56 2024

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