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Fluorine in PDB 6yti: CLK1 Bound with ETH1610 (Cpd 17)

Enzymatic activity of CLK1 Bound with ETH1610 (Cpd 17)

All present enzymatic activity of CLK1 Bound with ETH1610 (Cpd 17):
2.7.12.1;

Protein crystallography data

The structure of CLK1 Bound with ETH1610 (Cpd 17), PDB code: 6yti was solved by M.Schroeder, A.Chaikuad, S.Knapp, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.03 / 2.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.518, 63.873, 79.410, 90.00, 118.83, 90.00
R / Rfree (%) 19.5 / 25.6

Fluorine Binding Sites:

The binding sites of Fluorine atom in the CLK1 Bound with ETH1610 (Cpd 17) (pdb code 6yti). 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 CLK1 Bound with ETH1610 (Cpd 17), PDB code: 6yti:

Fluorine binding site 1 out of 1 in 6yti

Go back to Fluorine Binding Sites List in 6yti
Fluorine binding site 1 out of 1 in the CLK1 Bound with ETH1610 (Cpd 17)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of CLK1 Bound with ETH1610 (Cpd 17) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F605

b:70.9
occ:1.00
FAD A:7A7605 0.0 70.9 1.0
CAT A:7A7605 1.3 63.0 1.0
CAJ A:7A7605 2.3 68.2 1.0
CAU A:7A7605 2.3 54.5 1.0
NAN A:7A7605 2.7 47.8 1.0
CZ A:PHE172 3.1 62.4 1.0
C6 A:7A7605 3.3 45.2 1.0
N1 A:7A7605 3.3 41.2 1.0
CE2 A:PHE172 3.6 63.8 1.0
CAS A:7A7605 3.6 73.6 1.0
CAG A:7A7605 3.6 56.8 1.0
O A:GLU169 3.6 61.4 1.0
CG2 A:VAL175 3.8 37.7 1.0
CAF A:7A7605 4.1 65.2 1.0
O A:GLY168 4.1 51.8 1.0
C A:GLY168 4.2 53.7 1.0
CE1 A:PHE172 4.2 61.3 1.0
CA A:GLY168 4.3 52.8 1.0
CB A:VAL175 4.4 38.1 1.0
C5 A:7A7605 4.4 38.1 1.0
C2 A:7A7605 4.5 36.9 1.0
OAP A:7A7605 4.6 81.0 1.0
C A:GLU169 4.6 64.4 1.0
N A:GLU169 4.8 59.4 1.0
CD2 A:PHE172 4.9 62.6 1.0

Reference:

M.Schroder, A.N.Bullock, O.Fedorov, F.Bracher, A.Chaikuad, S.Knapp. Dfg-1 Residue Controls Inhibitor Binding Mode and Affinity, Providing A Basis For Rational Design of Kinase Inhibitor Selectivity. J.Med.Chem. V. 63 10224 2020.
ISSN: ISSN 0022-2623
PubMed: 32787076
DOI: 10.1021/ACS.JMEDCHEM.0C00898
Page generated: Fri Aug 2 04:46:34 2024

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