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Atomistry » Manganese » PDB 2v3z-2wgz » 2vxl | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 2v3z-2wgz » 2vxl » |
Manganese in PDB 2vxl: Screening A Limited Structure-Based Library Identifies Udp- Galnac-Specific Mutants of Alpha-1,3 GalactosyltransferaseEnzymatic activity of Screening A Limited Structure-Based Library Identifies Udp- Galnac-Specific Mutants of Alpha-1,3 Galactosyltransferase
All present enzymatic activity of Screening A Limited Structure-Based Library Identifies Udp- Galnac-Specific Mutants of Alpha-1,3 Galactosyltransferase:
2.4.1.87; Protein crystallography data
The structure of Screening A Limited Structure-Based Library Identifies Udp- Galnac-Specific Mutants of Alpha-1,3 Galactosyltransferase, PDB code: 2vxl
was solved by
P.Tumbale,
H.Jamaluddin,
N.Thiyagarajan,
K.R.Acharya,
K.Brew,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Manganese Binding Sites:
The binding sites of Manganese atom in the Screening A Limited Structure-Based Library Identifies Udp- Galnac-Specific Mutants of Alpha-1,3 Galactosyltransferase
(pdb code 2vxl). 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 Screening A Limited Structure-Based Library Identifies Udp- Galnac-Specific Mutants of Alpha-1,3 Galactosyltransferase, PDB code: 2vxl: Manganese binding site 1 out of 1 in 2vxlGo back to Manganese Binding Sites List in 2vxl
Manganese binding site 1 out
of 1 in the Screening A Limited Structure-Based Library Identifies Udp- Galnac-Specific Mutants of Alpha-1,3 Galactosyltransferase
Mono view Stereo pair view
Reference:
P.Tumbale,
H.Jamaluddin,
N.Thiyagarajan,
K.R.Acharya,
K.Brew.
Screening A Limited Structure-Based Library Identifies Udp-Galnac-Specific Mutants of {Alpha}- 1,3-Galactosyltransferase. Glycobiology V. 18 1036 2008.
Page generated: Sat Oct 5 15:20:00 2024
ISSN: ISSN 0959-6658 PubMed: 18782853 DOI: 10.1093/GLYCOB/CWN083 |
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