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Chlorine in PDB 5ory: 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: 5ory 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) 71.14 / 1.99
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 82.140, 82.140, 176.250, 90.00, 90.00, 120.00
R / Rfree (%) 20.4 / 26.5

Other elements in 5ory:

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

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

Chlorine binding site 1 out of 3 in 5ory

Go back to Chlorine Binding Sites List in 5ory
Chlorine 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 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:81.1
occ:0.41
N A:SER284 3.2 77.7 1.0
CB A:SER284 3.5 75.1 1.0
CA A:SER284 3.8 77.6 1.0
OG A:SER283 3.9 82.3 1.0
OG A:SER284 4.0 80.0 1.0
O A:SER284 4.1 86.1 1.0
C A:SER284 4.2 84.3 1.0
C A:SER283 4.2 70.8 1.0
NE A:ARG286 4.2 0.8 1.0
CA A:SER283 4.3 74.5 1.0
NH2 A:ARG286 4.6 0.7 1.0
CZ A:ARG286 4.7 0.0 1.0
CB A:SER283 4.7 69.2 1.0
CG A:ARG286 4.8 0.7 1.0
CD A:ARG286 5.0 0.3 1.0

Chlorine binding site 2 out of 3 in 5ory

Go back to Chlorine Binding Sites List in 5ory
Chlorine 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 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:Cl405

b:97.2
occ:1.00
N A:ARG286 3.2 0.4 1.0
NH2 A:ARG255 3.5 73.1 1.0
OG1 A:THR287 3.5 0.2 1.0
N A:THR287 3.7 0.8 1.0
CA A:ARG285 4.0 0.6 1.0
CA A:ARG286 4.1 0.8 1.0
CB A:ARG286 4.1 0.3 1.0
C A:ARG285 4.1 0.9 1.0
CZ3 A:TRP277 4.1 60.8 1.0
CG A:ARG285 4.3 91.1 1.0
CB A:THR287 4.3 0.8 1.0
NH1 A:ARG255 4.3 62.1 1.0
O A:SER284 4.4 86.1 1.0
C A:ARG286 4.4 0.0 1.0
CZ A:ARG255 4.4 66.9 1.0
NH2 A:ARG180 4.4 0.6 1.0
CG A:ARG286 4.5 0.7 1.0
CE3 A:TRP277 4.6 61.3 1.0
CA A:THR287 4.6 0.2 1.0
NH1 A:ARG180 4.7 0.6 1.0
CB A:ARG285 4.7 94.5 1.0

Chlorine binding site 3 out of 3 in 5ory

Go back to Chlorine Binding Sites List in 5ory
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl407

b:0.4
occ:1.00
N A:PHE165 2.6 54.8 1.0
O A:PHE144 3.0 88.2 1.0
OE1 A:GLN168 3.1 0.2 1.0
CA A:PHE165 3.5 61.9 1.0
CB A:PHE165 3.5 54.9 1.0
O A:PHE165 3.5 61.0 1.0
C A:LEU164 3.5 55.6 1.0
CB A:PHE144 3.5 77.7 1.0
CA A:PHE144 3.6 85.6 1.0
C A:PHE144 3.6 87.6 1.0
CA A:LEU164 3.6 57.8 1.0
CD A:GLN168 3.6 0.5 1.0
CD2 A:PHE165 3.8 73.7 1.0
CB A:GLN168 3.8 62.7 1.0
C A:PHE165 3.9 59.4 1.0
CB A:LEU164 4.0 57.0 1.0
O A:HOH541 4.1 71.1 1.0
CG A:PHE165 4.1 72.4 1.0
CD1 A:PHE144 4.2 73.1 1.0
CG A:GLN168 4.2 85.8 1.0
NE2 A:GLN168 4.3 0.8 1.0
CG A:PHE144 4.4 74.3 1.0
O A:LEU164 4.7 52.7 1.0
N A:GLY145 4.8 78.1 1.0
CG A:LEU169 4.8 51.4 1.0
O A:VAL163 4.8 48.0 1.0
N A:LEU164 4.9 56.5 1.0
CG A:LEU164 4.9 65.8 1.0
N A:PHE144 5.0 78.1 1.0
CD2 A:LEU164 5.0 67.8 1.0
CE2 A:PHE165 5.0 76.8 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: Fri Jul 26 14:43:08 2024

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