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Fluorine in PDB 5orr: 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: 5orr 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) 65.98 / 2.09
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 82.140, 82.140, 176.500, 90.00, 90.00, 120.00
R / Rfree (%) 19.9 / 25.6

Other elements in 5orr:

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
Chlorine (Cl) 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 5orr). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment, PDB code: 5orr:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in 5orr

Go back to Fluorine Binding Sites List in 5orr
Fluorine binding site 1 out of 3 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:90.6
occ:1.00
F2 A:A5Q404 0.0 90.6 1.0
C8 A:A5Q404 1.3 93.0 1.0
F1 A:A5Q404 2.1 96.9 1.0
F A:A5Q404 2.1 88.0 1.0
C5 A:A5Q404 2.4 97.9 1.0
C4 A:A5Q404 2.8 95.3 1.0
CE2 A:TYR199 3.1 82.4 1.0
CZ A:TYR199 3.3 87.2 1.0
OH A:TYR199 3.5 90.9 1.0
C6 A:A5Q404 3.6 98.8 1.0
CD2 A:TYR199 3.7 72.0 1.0
CE1 A:TYR199 4.1 77.1 1.0
C3 A:A5Q404 4.1 93.1 1.0
CG A:TYR199 4.5 63.7 1.0
CD1 A:TYR199 4.6 63.5 1.0
C7 A:A5Q404 4.7 98.1 1.0
CG A:ARG179 4.7 68.8 1.0
NE A:ARG179 4.9 72.8 1.0
C2 A:A5Q404 5.0 97.8 1.0

Fluorine binding site 2 out of 3 in 5orr

Go back to Fluorine Binding Sites List in 5orr
Fluorine binding site 2 out of 3 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 2 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:88.0
occ:1.00
F A:A5Q404 0.0 88.0 1.0
C8 A:A5Q404 1.3 93.0 1.0
F1 A:A5Q404 2.1 96.9 1.0
F2 A:A5Q404 2.1 90.6 1.0
C5 A:A5Q404 2.4 97.9 1.0
CD2 A:TYR199 3.1 72.0 1.0
C6 A:A5Q404 3.2 98.8 1.0
C4 A:A5Q404 3.2 95.3 1.0
CE2 A:TYR199 3.4 82.4 1.0
CG A:TYR199 3.6 63.7 1.0
CG2 A:VAL182 3.8 53.9 1.0
CZ A:TYR199 4.0 87.2 1.0
CD1 A:TYR199 4.1 63.5 1.0
CB A:TYR199 4.2 61.0 1.0
CG1 A:VAL206 4.2 45.8 1.0
CE1 A:TYR199 4.3 77.1 1.0
C7 A:A5Q404 4.4 98.1 1.0
C3 A:A5Q404 4.4 93.1 1.0
CB A:VAL182 4.6 50.9 1.0
CG1 A:VAL182 4.8 50.3 1.0
OH A:TYR199 4.8 90.9 1.0
CD2 A:LEU208 4.8 39.0 1.0
CG A:LEU178 4.9 55.6 1.0
C2 A:A5Q404 5.0 97.8 1.0
CD2 A:LEU178 5.0 57.2 1.0

Fluorine binding site 3 out of 3 in 5orr

Go back to Fluorine Binding Sites List in 5orr
Fluorine binding site 3 out of 3 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 3 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:96.9
occ:1.00
F1 A:A5Q404 0.0 96.9 1.0
C8 A:A5Q404 1.3 93.0 1.0
F2 A:A5Q404 2.1 90.6 1.0
F A:A5Q404 2.1 88.0 1.0
C5 A:A5Q404 2.4 97.9 1.0
C6 A:A5Q404 2.8 98.8 1.0
CG A:ARG179 3.4 68.8 1.0
C4 A:A5Q404 3.6 95.3 1.0
CA A:ARG179 3.6 51.8 1.0
CG2 A:VAL182 3.9 53.9 1.0
CB A:ARG179 4.0 55.4 1.0
N A:ARG179 4.0 49.3 1.0
C7 A:A5Q404 4.1 98.1 1.0
CB A:VAL182 4.2 50.9 1.0
O A:LEU178 4.2 45.3 1.0
CD A:ARG179 4.3 73.9 1.0
C A:LEU178 4.3 54.2 1.0
NE A:ARG179 4.6 72.8 1.0
CG1 A:VAL182 4.6 50.3 1.0
C3 A:A5Q404 4.7 93.1 1.0
CE2 A:TYR199 4.7 82.4 1.0
C A:ARG179 4.8 51.9 1.0
CG A:LEU178 4.8 55.6 1.0
CZ A:TYR199 4.9 87.2 1.0
O A:ARG179 4.9 52.5 1.0
CD2 A:TYR199 4.9 72.0 1.0
C2 A:A5Q404 5.0 97.8 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: Tue Jul 15 05:54:24 2025

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