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Atomistry » Chlorine » PDB 5xvg-5y7d » 5y25 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 5xvg-5y7d » 5y25 » |
Chlorine in PDB 5y25: Egfr Kinase Domain Mutant (T790M/L858R) with Covalent Ligand Ns-062Enzymatic activity of Egfr Kinase Domain Mutant (T790M/L858R) with Covalent Ligand Ns-062
All present enzymatic activity of Egfr Kinase Domain Mutant (T790M/L858R) with Covalent Ligand Ns-062:
2.7.10.1; Protein crystallography data
The structure of Egfr Kinase Domain Mutant (T790M/L858R) with Covalent Ligand Ns-062, PDB code: 5y25
was solved by
M.Shiroishi,
Y.Abe,
J.M.M.Caaveiro,
S.Sakamoto,
S.Morimoto,
H.Fuchida,
N.Shindo,
A.Ojida,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5y25:
The structure of Egfr Kinase Domain Mutant (T790M/L858R) with Covalent Ligand Ns-062 also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Egfr Kinase Domain Mutant (T790M/L858R) with Covalent Ligand Ns-062
(pdb code 5y25). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Egfr Kinase Domain Mutant (T790M/L858R) with Covalent Ligand Ns-062, PDB code: 5y25: Chlorine binding site 1 out of 1 in 5y25Go back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Egfr Kinase Domain Mutant (T790M/L858R) with Covalent Ligand Ns-062
![]() Mono view ![]() Stereo pair view
Reference:
N.Shindo,
H.Fuchida,
M.Sato,
K.Watari,
T.Shibata,
K.Kuwata,
C.Miura,
K.Okamoto,
Y.Hatsuyama,
K.Tokunaga,
S.Sakamoto,
S.Morimoto,
Y.Abe,
M.Shiroishi,
J.M.M.Caaveiro,
T.Ueda,
T.Tamura,
N.Matsunaga,
T.Nakao,
S.Koyanagi,
S.Ohdo,
Y.Yamaguchi,
I.Hamachi,
M.Ono,
A.Ojida.
Selective and Reversible Modification of Kinase Cysteines with Chlorofluoroacetamides. Nat.Chem.Biol. V. 15 250 2019.
Page generated: Sat Jul 12 10:50:21 2025
ISSN: ESSN 1552-4469 PubMed: 30643284 DOI: 10.1038/S41589-018-0204-3 |
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