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Atomistry » Chlorine » PDB 1zch-1zoh » 1zi4 » |
Chlorine in PDB 1zi4: Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with H Type II TrisaccharideEnzymatic activity of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with H Type II Trisaccharide
All present enzymatic activity of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with H Type II Trisaccharide:
2.4.1.40; Protein crystallography data
The structure of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with H Type II Trisaccharide, PDB code: 1zi4
was solved by
J.A.Letts,
N.L.Rose,
Y.R.Fang,
C.H.Barry,
S.N.Borisova,
N.O.Seto,
M.M.Palcic,
S.V.Evans,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1zi4:
The structure of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with H Type II Trisaccharide also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with H Type II Trisaccharide
(pdb code 1zi4). 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 Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with H Type II Trisaccharide, PDB code: 1zi4: Chlorine binding site 1 out of 1 in 1zi4Go back to Chlorine Binding Sites List in 1zi4
Chlorine binding site 1 out
of 1 in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with H Type II Trisaccharide
Mono view Stereo pair view
Reference:
J.A.Letts,
N.L.Rose,
Y.R.Fang,
C.H.Barry,
S.N.Borisova,
N.O.Seto,
M.M.Palcic,
S.V.Evans.
Differential Recognition of the Type I and II H Antigen Acceptors By the Human Abo(H) Blood Group A and B Glycosyltransferases. J.Biol.Chem. V. 281 3625 2006.
Page generated: Sat Dec 12 08:57:00 2020
ISSN: ISSN 0021-9258 PubMed: 16326711 DOI: 10.1074/JBC.M507620200 |
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