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Atomistry » Bromine » PDB 5mrm-5o0j » 5nra » |
Bromine in PDB 5nra: Crystal Structure of Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7GEnzymatic activity of Crystal Structure of Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7G
All present enzymatic activity of Crystal Structure of Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7G:
3.2.1.14; Protein crystallography data
The structure of Crystal Structure of Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7G, PDB code: 5nra
was solved by
M.Mazur,
J.Olczak,
S.Olejniczak,
R.Koralewski,
W.Czestkowski,
A.Jedrzejczak,
J.Golab,
K.Dzwonek,
B.Dymek,
P.Sklepkiewicz,
A.Zagozdzon,
T.Noonan,
K.Mahboubi,
B.Conway,
R.Sheeler,
P.Beckett,
W.M.Hungerford,
A.Podjarny,
A.Mitschler,
A.Cousido-Siah,
F.Fadel,
A.Golebiowski,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Bromine Binding Sites:
The binding sites of Bromine atom in the Crystal Structure of Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7G
(pdb code 5nra). This binding sites where shown within
5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7G, PDB code: 5nra: Bromine binding site 1 out of 1 in 5nraGo back to Bromine Binding Sites List in 5nra
Bromine binding site 1 out
of 1 in the Crystal Structure of Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7G
Mono view Stereo pair view
Reference:
M.Mazur,
J.Olczak,
S.Olejniczak,
R.Koralewski,
W.Czestkowski,
A.Jedrzejczak,
J.Golab,
K.Dzwonek,
B.Dymek,
P.L.Sklepkiewicz,
A.Zagozdzon,
T.Noonan,
K.Mahboubi,
B.Conway,
R.Sheeler,
P.Beckett,
W.M.Hungerford,
A.Podjarny,
A.Mitschler,
A.Cousido-Siah,
F.Fadel,
A.Golebiowski.
Targeting Acidic Mammalian Chitinase Is Effective in Animal Model of Asthma. J. Med. Chem. V. 61 695 2018.
Page generated: Sat Dec 12 02:28:36 2020
ISSN: ISSN 1520-4804 PubMed: 29283260 DOI: 10.1021/ACS.JMEDCHEM.7B01051 |
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