Chlorine in PDB 5orx: 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: 5orx 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) 66.07 / 1.88
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 82.400, 82.400, 174.810, 90.00, 90.00, 120.00
R / Rfree (%) 22 / 27

Other elements in 5orx:

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

Chlorine binding site 1 out of 2 in 5orx

Go back to Chlorine Binding Sites List in 5orx
Chlorine binding site 1 out of 2 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:51.1
occ:1.00
CL1 A:A6H404 0.0 51.1 1.0
C9 A:A6H404 1.7 50.0 1.0
C4 A:A6H404 2.7 46.0 1.0
C8 A:A6H404 2.7 49.0 1.0
O A:A6H404 2.9 44.7 1.0
O A:GLU175 3.4 38.6 1.0
C3 A:A6H404 3.7 50.7 1.0
CB A:GLU175 3.8 42.3 1.0
CA A:GLU175 3.8 40.8 1.0
CD2 A:LEU178 3.9 51.6 1.0
C5 A:A6H404 4.0 48.4 1.0
C7 A:A6H404 4.0 53.5 1.0
CZ A:ARG179 4.0 67.5 1.0
CB A:LEU178 4.0 37.4 1.0
C A:GLU175 4.0 41.9 1.0
CG A:ARG179 4.0 43.8 1.0
N1 A:A6H404 4.0 46.9 1.0
NH2 A:ARG179 4.1 68.9 1.0
NE A:ARG179 4.1 58.7 1.0
CD1 A:LEU178 4.2 39.2 1.0
CG A:LEU178 4.3 40.6 1.0
CG A:GLU175 4.3 43.4 1.0
NH1 A:ARG179 4.5 60.5 1.0
C6 A:A6H404 4.5 48.6 1.0
C2 A:A6H404 4.5 49.1 1.0
O A:HOH543 4.5 48.7 1.0
CD A:ARG179 4.7 52.1 1.0
N A:ARG179 4.7 37.8 1.0

Chlorine binding site 2 out of 2 in 5orx

Go back to Chlorine Binding Sites List in 5orx
Chlorine binding site 2 out of 2 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 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:Cl404

b:52.1
occ:1.00
CL A:A6H404 0.0 52.1 1.0
C5 A:A6H404 1.7 48.4 1.0
C4 A:A6H404 2.7 46.0 1.0
C6 A:A6H404 2.7 48.6 1.0
O A:A6H404 3.0 44.7 1.0
CD2 A:HIS201 3.3 49.8 1.0
CG A:HIS201 3.4 48.7 1.0
C3 A:A6H404 3.4 50.7 1.0
N1 A:A6H404 3.6 46.9 1.0
CB A:HIS201 3.8 44.3 1.0
CE2 A:TYR199 3.9 46.8 1.0
NE2 A:HIS201 3.9 46.9 1.0
ND1 A:HIS201 4.0 51.6 1.0
C9 A:A6H404 4.0 50.0 1.0
C7 A:A6H404 4.0 53.5 1.0
CG2 A:VAL206 4.0 36.9 1.0
CE1 A:HIS201 4.2 49.6 1.0
CD2 A:TYR199 4.2 46.5 1.0
CG1 A:VAL206 4.3 35.8 1.0
C2 A:A6H404 4.4 49.1 1.0
O A:HOH543 4.5 48.7 1.0
C8 A:A6H404 4.5 49.0 1.0
C10 A:A6H404 4.6 46.4 1.0
CB A:VAL206 4.8 37.6 1.0
CZ A:TYR199 5.0 50.1 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: Sat Dec 12 12:13:30 2020

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