Fluorine in PDB 3rgf: Crystal Structure of Human CDK8/Cycc

All present enzymatic activity of Crystal Structure of Human CDK8/Cycc:
2.7.11.22; 2.7.11.23;

The structure of Crystal Structure of Human CDK8/Cycc, PDB code: 3rgf was solved by E.V.Schneider, J.Boettcher, M.Blaesse, R.Huber, K.Maskos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.57 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	70.690, 70.610, 79.140, 90.00, 108.31, 90.00
R / Rfree (%)	18 / 22.1

The structure of Crystal Structure of Human CDK8/Cycc also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of Human CDK8/Cycc (pdb code 3rgf). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of Human CDK8/Cycc, PDB code: 3rgf:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Human CDK8/Cycc


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 Human CDK8/Cycc within 5.0Å range: probe atom residue distance (Å) B Occ A:F465 b:40.0 occ:1.00 F8 A:BAX465 0.0 40.0 1.0 C7 A:BAX465 1.3 40.6 1.0 F9 A:BAX465 2.2 40.3 1.0 F10 A:BAX465 2.2 41.8 1.0 C6 A:BAX465 2.4 40.5 1.0 C1 A:BAX465 2.8 40.5 1.0 O A:ILE171 3.3 32.1 1.0 CG1 A:VAL78 3.5 31.1 1.0 C5 A:BAX465 3.7 40.5 1.0 C A:ILE171 3.9 30.7 1.0 CA A:ALA172 4.0 32.4 1.0 CG2 A:ILE171 4.2 27.6 1.0 C2 A:BAX465 4.2 33.6 1.0 C A:ALA172 4.3 33.0 1.0 N A:ALA172 4.3 31.9 1.0 CL11 A:BAX465 4.4 48.5 1.0 N A:ASP173 4.4 36.5 1.0 O15 A:BAX465 4.5 32.9 1.0 CG2 A:ILE79 4.5 38.0 1.0 CD2 A:LEU70 4.6 39.1 1.0 CB A:ILE171 4.6 30.3 1.0 CB A:VAL78 4.7 33.9 1.0 N A:ILE79 4.8 34.1 1.0 O A:ALA172 4.8 33.2 1.0 CD1 A:LEU142 4.8 27.8 1.0 C4 A:BAX465 4.8 36.1 1.0 CB A:ASP173 4.9 42.9 1.0 CD2 A:HIS149 4.9 29.3 1.0 CA A:ILE171 5.0 31.1 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Human CDK8/Cycc


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 Human CDK8/Cycc within 5.0Å range: probe atom residue distance (Å) B Occ A:F465 b:40.3 occ:1.00 F9 A:BAX465 0.0 40.3 1.0 C7 A:BAX465 1.3 40.6 1.0 F8 A:BAX465 2.2 40.0 1.0 F10 A:BAX465 2.2 41.8 1.0 C6 A:BAX465 2.4 40.5 1.0 CL11 A:BAX465 2.9 48.5 1.0 C5 A:BAX465 2.9 40.5 1.0 CD2 A:LEU142 3.4 24.6 1.0 C1 A:BAX465 3.5 40.5 1.0 CG1 A:VAL78 3.6 31.1 1.0 CD1 A:LEU73 3.6 41.2 1.0 CD1 A:LEU142 3.9 27.8 1.0 CG A:LEU142 4.2 30.0 1.0 C4 A:BAX465 4.2 36.1 1.0 CD2 A:LEU70 4.6 39.1 1.0 C2 A:BAX465 4.7 33.6 1.0 CB A:VAL78 4.9 33.9 1.0 C3 A:BAX465 4.9 36.6 1.0 CG A:LEU73 5.0 38.1 1.0 CG1 A:VAL147 5.0 33.0 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Human CDK8/Cycc


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 Human CDK8/Cycc within 5.0Å range: probe atom residue distance (Å) B Occ A:F465 b:41.8 occ:1.00 F10 A:BAX465 0.0 41.8 1.0 C7 A:BAX465 1.4 40.6 1.0 F9 A:BAX465 2.2 40.3 1.0 F8 A:BAX465 2.2 40.0 1.0 C6 A:BAX465 2.3 40.5 1.0 C5 A:BAX465 2.9 40.5 1.0 CL11 A:BAX465 3.0 48.5 1.0 CD2 A:HIS149 3.4 29.3 1.0 C1 A:BAX465 3.4 40.5 1.0 CD1 A:LEU142 3.7 27.8 1.0 NE2 A:HIS149 4.0 30.3 1.0 CG2 A:ILE171 4.2 27.6 1.0 CB A:ASP173 4.2 42.9 1.0 C4 A:BAX465 4.2 36.1 1.0 CG A:HIS149 4.2 28.8 1.0 C2 A:BAX465 4.5 33.6 1.0 CD2 A:LEU142 4.6 24.6 1.0 C A:ALA172 4.6 33.0 1.0 N A:ASP173 4.7 36.5 1.0 CB A:HIS149 4.7 29.4 1.0 O A:ALA172 4.7 33.2 1.0 CG A:LEU142 4.8 30.0 1.0 CA A:HIS149 4.8 30.1 1.0 OD2 A:ASP173 4.9 61.7 1.0 C3 A:BAX465 4.9 36.6 1.0 O A:ILE171 5.0 32.1 1.0

E.V.Schneider, J.Bottcher, M.Blaesse, L.Neumann, R.Huber, K.Maskos. The Structure of CDK8/Cycc Implicates Specificity in the Cdk/Cyclin Family and Reveals Interaction with A Deep Pocket Binder. J.Mol.Biol. V. 412 251 2011.
ISSN: ISSN 0022-2836
PubMed: 21806996
DOI: 10.1016/J.JMB.2011.07.020