Fluorine in PDB 5c01: Crystal Structure of Kinase

All present enzymatic activity of Crystal Structure of Kinase:
2.7.10.2;

The structure of Crystal Structure of Kinase, PDB code: 5c01 was solved by X.Min, Z.Wang, N.Walker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.15
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.340, 48.170, 114.210, 90.00, 93.28, 90.00
R / Rfree (%)	19.5 / 24

The binding sites of Fluorine atom in the Crystal Structure of Kinase (pdb code 5c01). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Crystal Structure of Kinase, PDB code: 5c01:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Crystal Structure of Kinase


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 Kinase within 5.0Å range: probe atom residue distance (Å) B Occ A:F901 b:18.7 occ:1.00 F16 A:UNL901 0.0 18.7 1.0 C11 A:UNL901 1.4 19.0 1.0 C12 A:UNL901 2.4 19.7 1.0 C10 A:UNL901 2.4 19.3 1.0 C2 A:UNL901 2.9 18.8 1.0 C3 A:UNL901 3.0 18.4 1.0 CG1 A:VAL603 3.1 15.8 1.0 CB A:VAL603 3.3 15.7 1.0 C26 A:UNL901 3.3 19.3 1.0 C13 A:UNL901 3.7 19.5 1.0 C15 A:UNL901 3.7 20.2 1.0 CG2 A:VAL603 3.7 16.0 1.0 CB A:LEU595 3.7 17.4 1.0 N A:GLY596 3.9 18.6 1.0 C27 A:UNL901 4.0 19.4 1.0 C1 A:UNL901 4.0 19.3 1.0 C A:LEU595 4.1 17.8 1.0 C4 A:UNL901 4.2 18.3 1.0 C14 A:UNL901 4.2 19.9 1.0 CA A:GLY596 4.2 19.6 1.0 C A:GLY596 4.4 20.1 1.0 O A:LEU595 4.5 17.9 1.0 CD1 A:LEU595 4.5 17.4 1.0 O A:GLY596 4.6 20.0 1.0 CA A:LEU595 4.6 17.5 1.0 N19 A:UNL901 4.6 18.1 1.0 C25 A:UNL901 4.6 19.3 1.0 CA A:VAL603 4.7 15.6 1.0 O A:HOH1063 4.8 34.9 1.0 CG A:LEU595 4.8 17.4 1.0 F17 A:UNL901 4.8 21.8 1.0 O A:VAL603 4.9 15.3 1.0 C6 A:UNL901 5.0 18.4 1.0

Fluorine binding site 2 out of 4 in the Crystal Structure of Kinase


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 Kinase within 5.0Å range: probe atom residue distance (Å) B Occ A:F901 b:21.8 occ:1.00 F17 A:UNL901 0.0 21.8 1.0 C15 A:UNL901 1.3 20.2 1.0 C14 A:UNL901 2.3 19.9 1.0 C10 A:UNL901 2.4 19.3 1.0 C2 A:UNL901 2.9 18.8 1.0 C1 A:UNL901 2.9 19.3 1.0 C13 A:UNL901 3.6 19.5 1.0 C11 A:UNL901 3.7 19.0 1.0 O A:HOH1084 3.7 31.4 1.0 CG1 A:VAL697 4.0 21.2 1.0 CG A:PRO694 4.0 17.2 1.0 C3 A:UNL901 4.0 18.4 1.0 C6 A:UNL901 4.1 18.4 1.0 C12 A:UNL901 4.1 19.7 1.0 O A:HOH1063 4.2 34.9 1.0 O A:LEU595 4.7 17.9 1.0 F16 A:UNL901 4.8 18.7 1.0 CB A:PRO694 4.9 16.8 1.0 C4 A:UNL901 5.0 18.3 1.0 C5 A:UNL901 5.0 18.4 1.0 CD A:PRO694 5.0 16.7 1.0

Fluorine binding site 3 out of 4 in the Crystal Structure of Kinase


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 Kinase within 5.0Å range: probe atom residue distance (Å) B Occ B:F901 b:23.4 occ:1.00 F16 B:UNL901 0.0 23.4 1.0 C11 B:UNL901 1.3 23.9 1.0 C12 B:UNL901 2.3 24.5 1.0 C10 B:UNL901 2.4 24.8 1.0 C2 B:UNL901 2.8 24.3 1.0 C3 B:UNL901 3.0 24.3 1.0 CG1 B:VAL603 3.2 22.8 1.0 CB B:VAL603 3.3 22.4 1.0 C26 B:UNL901 3.4 24.6 1.0 C13 B:UNL901 3.6 25.0 1.0 C15 B:UNL901 3.6 25.3 1.0 CB B:LEU595 3.7 23.8 1.0 CG2 B:VAL603 3.9 22.2 1.0 C1 B:UNL901 4.0 24.5 1.0 N B:GLY596 4.0 25.9 1.0 C27 B:UNL901 4.1 25.6 1.0 C B:LEU595 4.1 24.9 1.0 C14 B:UNL901 4.1 25.3 1.0 C4 B:UNL901 4.1 23.8 1.0 CA B:GLY596 4.2 26.5 1.0 O B:LEU595 4.4 24.0 1.0 C B:GLY596 4.5 27.1 1.0 CD1 B:LEU595 4.5 22.9 1.0 CA B:LEU595 4.6 24.1 1.0 O B:GLY596 4.6 24.5 1.0 N19 B:UNL901 4.7 22.9 1.0 CA B:VAL603 4.7 21.9 1.0 O B:VAL603 4.7 22.7 1.0 C25 B:UNL901 4.7 24.9 1.0 CG B:LEU595 4.8 23.8 1.0 F17 B:UNL901 4.8 26.6 1.0 C6 B:UNL901 4.9 24.1 1.0 C B:VAL603 5.0 22.5 1.0 C5 B:UNL901 5.0 23.6 1.0 N B:GLN597 5.0 27.8 1.0

Fluorine binding site 4 out of 4 in the Crystal Structure of Kinase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of Kinase within 5.0Å range: probe atom residue distance (Å) B Occ B:F901 b:26.6 occ:1.00 F17 B:UNL901 0.0 26.6 1.0 C15 B:UNL901 1.3 25.3 1.0 C14 B:UNL901 2.4 25.3 1.0 C10 B:UNL901 2.4 24.8 1.0 C2 B:UNL901 2.9 24.3 1.0 C1 B:UNL901 2.9 24.5 1.0 NH2 B:ARG738 3.4 47.6 1.0 NE B:ARG738 3.5 43.3 1.0 C13 B:UNL901 3.6 25.0 1.0 C11 B:UNL901 3.7 23.9 1.0 CZ B:ARG738 3.9 45.5 1.0 CG B:PRO694 3.9 19.6 1.0 CG1 B:VAL697 4.0 21.9 1.0 C3 B:UNL901 4.0 24.3 1.0 C6 B:UNL901 4.1 24.1 1.0 C12 B:UNL901 4.1 24.5 1.0 CD B:ARG738 4.6 39.3 1.0 O B:LEU595 4.7 24.0 1.0 CB B:PRO694 4.8 19.3 1.0 F16 B:UNL901 4.8 23.4 1.0 CG B:ARG738 4.8 34.7 1.0 CD B:PRO694 4.9 19.2 1.0 C5 B:UNL901 5.0 23.6 1.0 C4 B:UNL901 5.0 23.8 1.0

X.Min, D.Ungureanu, S.Maxwell, H.Hammaren, S.Thibault, E.K.Hillert, M.Ayres, B.Greenfield, J.Eksterowicz, C.Gabel, N.Walker, O.Silvennoinen, Z.Wang. Structural and Functional Characterization of the JH2 Pseudokinase Domain of Jak Family Tyrosine Kinase 2 (TYK2). J.Biol.Chem. V. 290 27261 2015.
ISSN: ESSN 1083-351X
PubMed: 26359499
DOI: 10.1074/JBC.M115.672048