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Chlorine in PDB 5os0: 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: 5os0 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) 71.20 / 1.74
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 82.210, 82.210, 175.860, 90.00, 90.00, 120.00
R / Rfree (%) 21.7 / 26.4

Other elements in 5os0:

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 Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment (pdb code 5os0). 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 Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment, PDB code: 5os0:

Chlorine binding site 1 out of 1 in 5os0

Go back to Chlorine Binding Sites List in 5os0
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl404

b:0.6
occ:1.00
 CL1 A:A6Z404 0.0 0.6 1.0
C5 A:A6Z404 1.7 65.3 1.0
C4 A:A6Z404 2.6 63.1 1.0
C6 A:A6Z404 2.9 59.0 1.0
CD2 A:TYR199 3.0 62.9 1.0
CD2 A:HIS201 3.6 60.8 1.0
CG A:TYR199 3.6 65.8 1.0
CB A:TYR199 3.7 50.8 1.0
CE2 A:TYR199 3.8 66.2 1.0
N A:PHE200 3.9 46.5 1.0
O A:PHE200 3.9 43.8 1.0
CG1 A:VAL206 4.0 37.1 1.0
C A:PHE200 4.0 48.9 1.0
C3 A:A6Z404 4.1 63.3 1.0
CA A:PHE200 4.1 48.3 1.0
C1 A:A6Z404 4.1 57.6 1.0
C A:TYR199 4.2 45.3 1.0
CG A:HIS201 4.4 60.8 1.0
CB A:HIS201 4.6 55.5 1.0
N A:HIS201 4.6 52.1 1.0
NE2 A:HIS201 4.6 62.9 1.0
C2 A:A6Z404 4.6 58.3 1.0
CA A:TYR199 4.6 44.6 1.0
O A:TYR199 4.7 46.4 1.0
CD1 A:TYR199 4.8 63.5 1.0
O A:HOH635 4.9 56.7 1.0
CZ A:TYR199 4.9 80.0 1.0
C7 A:A6Z404 5.0 57.4 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: Fri Jul 26 14:44:07 2024

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