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Atomistry » Manganese » PDB 1w2c-1xie » 1xhb | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 1w2c-1xie » 1xhb » |
Manganese in PDB 1xhb: The Crystal Structure of Udp-Galnac: Polypeptide Alpha-N- Acetylgalactosaminyltransferase-T1Enzymatic activity of The Crystal Structure of Udp-Galnac: Polypeptide Alpha-N- Acetylgalactosaminyltransferase-T1
All present enzymatic activity of The Crystal Structure of Udp-Galnac: Polypeptide Alpha-N- Acetylgalactosaminyltransferase-T1:
2.4.1.41; Protein crystallography data
The structure of The Crystal Structure of Udp-Galnac: Polypeptide Alpha-N- Acetylgalactosaminyltransferase-T1, PDB code: 1xhb
was solved by
T.A.Fritz,
J.H.Hurley,
L.B.Trinh,
J.Shiloach,
L.A.Tabak,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1xhb:
The structure of The Crystal Structure of Udp-Galnac: Polypeptide Alpha-N- Acetylgalactosaminyltransferase-T1 also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the The Crystal Structure of Udp-Galnac: Polypeptide Alpha-N- Acetylgalactosaminyltransferase-T1
(pdb code 1xhb). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the The Crystal Structure of Udp-Galnac: Polypeptide Alpha-N- Acetylgalactosaminyltransferase-T1, PDB code: 1xhb: Manganese binding site 1 out of 1 in 1xhbGo back to Manganese Binding Sites List in 1xhb
Manganese binding site 1 out
of 1 in the The Crystal Structure of Udp-Galnac: Polypeptide Alpha-N- Acetylgalactosaminyltransferase-T1
Mono view Stereo pair view
Reference:
T.A.Fritz,
J.H.Hurley,
L.B.Trinh,
J.Shiloach,
L.A.Tabak.
The Beginnings of Mucin Biosynthesis: the Crystal Structure of Udp-Galnac:Polypeptide {Alpha}-N-Acetylgalactosaminyltransferase-T1 Proc.Natl.Acad.Sci.Usa V. 101 15307 2004.
Page generated: Tue Dec 15 03:57:50 2020
ISSN: ISSN 0027-8424 PubMed: 15486088 DOI: 10.1073/PNAS.0405657101 |
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