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Fluorine in PDB 5aac: Structure of C1156Y Mutant Human Anaplastic Lymphoma Kinase in Complex with Crizotinib

Enzymatic activity of Structure of C1156Y Mutant Human Anaplastic Lymphoma Kinase in Complex with Crizotinib

All present enzymatic activity of Structure of C1156Y Mutant Human Anaplastic Lymphoma Kinase in Complex with Crizotinib:
2.7.10.1;

Protein crystallography data

The structure of Structure of C1156Y Mutant Human Anaplastic Lymphoma Kinase in Complex with Crizotinib, PDB code: 5aac was solved by M.Mctigue, Y.Deng, W.Liu, A.Brooun, A.Stewart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.66 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.541, 57.449, 104.787, 90.00, 90.00, 90.00
R / Rfree (%) 20.7 / 23.2

Other elements in 5aac:

The structure of Structure of C1156Y Mutant Human Anaplastic Lymphoma Kinase in Complex with Crizotinib also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Structure of C1156Y Mutant Human Anaplastic Lymphoma Kinase in Complex with Crizotinib (pdb code 5aac). 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 Structure of C1156Y Mutant Human Anaplastic Lymphoma Kinase in Complex with Crizotinib, PDB code: 5aac:

Fluorine binding site 1 out of 1 in 5aac

Go back to Fluorine Binding Sites List in 5aac
Fluorine binding site 1 out of 1 in the Structure of C1156Y Mutant Human Anaplastic Lymphoma Kinase in Complex with Crizotinib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of C1156Y Mutant Human Anaplastic Lymphoma Kinase in Complex with Crizotinib within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F9000

b:48.2
occ:1.00
F A:VGH9000 0.0 48.2 1.0
C12 A:VGH9000 1.3 49.2 1.0
C2 A:VGH9000 2.4 48.5 1.0
C18 A:VGH9000 2.4 49.2 1.0
CL2 A:VGH9000 3.0 57.0 1.0
N A:ASP1270 3.3 26.3 1.0
O A:ASN1254 3.3 21.2 1.0
C A:GLY1269 3.4 28.2 1.0
CA A:GLY1269 3.5 25.5 1.0
C A:ASN1254 3.5 18.5 1.0
CB A:ASP1270 3.6 28.2 1.0
CG A:LEU1256 3.6 23.2 1.0
C3 A:VGH9000 3.7 48.0 1.0
C17 A:VGH9000 3.8 48.2 1.0
CA A:ASN1254 3.8 18.5 1.0
CD1 A:LEU1256 3.9 27.5 1.0
CA A:ASP1270 3.9 25.9 1.0
CD2 A:LEU1256 4.0 25.6 1.0
N A:GLY1269 4.0 21.2 1.0
O A:GLY1269 4.1 32.4 1.0
O A:ARG1253 4.2 20.0 1.0
C13 A:VGH9000 4.2 48.1 1.0
N A:CYS1255 4.2 18.0 1.0
C A:CYS1255 4.6 19.7 1.0
CB A:ASN1254 4.7 18.3 1.0
CA A:CYS1255 4.7 17.8 1.0
O A:CYS1255 4.8 20.5 1.0
N A:ASN1254 4.8 17.7 1.0
CG A:ASP1270 4.9 32.2 1.0
CB A:LEU1256 4.9 20.4 1.0
C A:ARG1253 4.9 19.5 1.0
N A:LEU1256 5.0 18.1 1.0

Reference:

A.T.Shaw, L.Friboulet, I.Leshchiner, J.F.Gainor, S.Bergqvist, A.Brooun, B.J.Burke, Y.Deng, W.Liu, L.Dardaei, R.L.Frias, K.R.Schultz, J.Logan, L.P.James, T.Smeal, S.Timofeevski, R.Katayama, A.J.Iafrate, L.Le, M.Mctigue, G.Getz, T.W.Johnson, J.A.Engelman. Resensitization to Crizotinib By the Lorlatinib Alk Resistance Mutation L1198F. N.Engl.J.Med. V. 374 54 2016.
ISSN: ISSN 0028-4793
PubMed: 26698910
DOI: 10.1056/NEJMOA1508887
Page generated: Sun Dec 13 12:18:00 2020

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