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Atomistry » Manganese » PDB 1g15-1hkd » 1g15 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 1g15-1hkd » 1g15 » |
Manganese in PDB 1g15: Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active SiteEnzymatic activity of Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site
All present enzymatic activity of Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site:
3.1.26.4; Protein crystallography data
The structure of Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site, PDB code: 1g15
was solved by
E.R.Goedken,
S.Marqusee,
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 Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site
(pdb code 1g15). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site, PDB code: 1g15: Jump to Manganese binding site number: 1; 2; Manganese binding site 1 out of 2 in 1g15Go back to Manganese Binding Sites List in 1g15
Manganese binding site 1 out
of 2 in the Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site
Mono view Stereo pair view
Manganese binding site 2 out of 2 in 1g15Go back to Manganese Binding Sites List in 1g15
Manganese binding site 2 out
of 2 in the Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site
Mono view Stereo pair view
Reference:
E.R.Goedken,
S.Marqusee.
Co-Crystal of Escherichia Coli Rnase Hi with MN2+ Ions Reveals Two Divalent Metals Bound in the Active Site. J.Biol.Chem. V. 276 7266 2001.
Page generated: Sat Oct 5 10:31:31 2024
ISSN: ISSN 0021-9258 PubMed: 11083878 DOI: 10.1074/JBC.M009626200 |
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