Fluorine »
PDB 3qrj-3rgf »
3rcd »
Fluorine in PDB 3rcd: HER2 Kinase Domain Complexed with Tak-285
Enzymatic activity of HER2 Kinase Domain Complexed with Tak-285
All present enzymatic activity of HER2 Kinase Domain Complexed with Tak-285:
2.7.10.1;
2.7.10.1;
Protein crystallography data
The structure of HER2 Kinase Domain Complexed with Tak-285, PDB code: 3rcd
was solved by
K.Aertgeerts,
R.Skene,
S.Sogabe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 40.00 / 3.21 |
| Space group | P 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 50.542, 64.936, 92.360, 90.42, 89.72, 90.35 |
| R / Rfree (%) | 22.4 / 29.4 |
Other elements in 3rcd:
The structure of HER2 Kinase Domain Complexed with Tak-285 also contains other interesting chemical elements:
| Chlorine | (Cl) | 2 atoms |
Fluorine Binding Sites:
The binding sites of Fluorine atom in the HER2 Kinase Domain Complexed with Tak-285
(pdb code 3rcd). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the HER2 Kinase Domain Complexed with Tak-285, PDB code: 3rcd:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;
In total 6 binding sites of Fluorine where determined in the HER2 Kinase Domain Complexed with Tak-285, PDB code: 3rcd:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;
Fluorine binding site 1 out of 6 in 3rcd
Go back to
Fluorine Binding Sites List in 3rcd
Fluorine binding site 1 out
of 6 in the HER2 Kinase Domain Complexed with Tak-285
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 1 of HER2 Kinase Domain Complexed with Tak-285 within 5.0Å range:
|
Fluorine binding site 2 out of 6 in 3rcd
Go back to
Fluorine Binding Sites List in 3rcd
Fluorine binding site 2 out
of 6 in the HER2 Kinase Domain Complexed with Tak-285
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 2 of HER2 Kinase Domain Complexed with Tak-285 within 5.0Å range:
|
Fluorine binding site 3 out of 6 in 3rcd
Go back to
Fluorine Binding Sites List in 3rcd
Fluorine binding site 3 out
of 6 in the HER2 Kinase Domain Complexed with Tak-285
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 3 of HER2 Kinase Domain Complexed with Tak-285 within 5.0Å range:
|
Fluorine binding site 4 out of 6 in 3rcd
Go back to
Fluorine Binding Sites List in 3rcd
Fluorine binding site 4 out
of 6 in the HER2 Kinase Domain Complexed with Tak-285
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 4 of HER2 Kinase Domain Complexed with Tak-285 within 5.0Å range:
|
Fluorine binding site 5 out of 6 in 3rcd
Go back to
Fluorine Binding Sites List in 3rcd
Fluorine binding site 5 out
of 6 in the HER2 Kinase Domain Complexed with Tak-285
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 5 of HER2 Kinase Domain Complexed with Tak-285 within 5.0Å range:
|
Fluorine binding site 6 out of 6 in 3rcd
Go back to
Fluorine Binding Sites List in 3rcd
Fluorine binding site 6 out
of 6 in the HER2 Kinase Domain Complexed with Tak-285
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 6 of HER2 Kinase Domain Complexed with Tak-285 within 5.0Å range:
|
Reference:
T.Ishikawa,
M.Seto,
H.Banno,
Y.Kawakita,
M.Oorui,
T.Taniguchi,
Y.Ohta,
T.Tamura,
A.Nakayama,
H.Miki,
H.Kamiguchi,
T.Tanaka,
N.Habuka,
S.Sogabe,
J.Yano,
K.Aertgeerts,
K.Kamiyama.
Design and Synthesis of Novel Human Epidermal Growth Factor Receptor 2 (HER2)/Epidermal Growth Factor Receptor (Egfr) Dual Inhibitors Bearing A Pyrrolo[3,2-D]Pyrimidine Scaffold. J.Med.Chem. V. 54 8030 2011.
ISSN: ISSN 0022-2623
PubMed: 22003817
DOI: 10.1021/JM2008634
Page generated: Wed Jul 31 22:15:54 2024
ISSN: ISSN 0022-2623
PubMed: 22003817
DOI: 10.1021/JM2008634
Last articles
Zn in 9JYWZn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
