1v96

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v96 OCA], [http://www.ebi.ac.uk/pdbsum/1v96 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v96 RCSB]</span>
}}
}}
Line 25: Line 28:
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Tahirov, T H.]]
[[Category: Tahirov, T H.]]
-
[[Category: GOL]]
 
[[Category: nucleotide binding protein]]
[[Category: nucleotide binding protein]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: riken structural genomics/proteomics initiative]]
Line 33: Line 35:
[[Category: trna synthetase]]
[[Category: trna synthetase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:42:30 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:21:11 2008''

Revision as of 21:21, 30 March 2008


PDB ID 1v96

Drag the structure with the mouse to rotate
, resolution 1.75Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of hypothetical protein of unknown function from pyrococcus horikoshii OT3


Overview

The Pyrococcus horikoshii OT3 protein PH0500 is highly conserved within the Pyrococcus genus of hyperthermophilic archaea and shows low amino-acid sequence similarity with a family of PIN-domain proteins. The protein has been expressed, purified and crystallized in two crystal forms: PH0500-I and PH0500-II. The structure was determined at 2.0 A by the multiple anomalous dispersion method using a selenomethionyl derivative of crystal form PH0500-I (PH0500-I-Se). The structure of PH0500-I has been refined at 1.75 A resolution to an R factor of 20.9% and the structure of PH0500-II has been refined at 2.0 A resolution to an R factor of 23.4%. In both crystal forms as well as in solution the molecule appears to be a dimer. Searches of the databases for protein-fold similarities confirmed that the PH0500 protein is a PIN-domain protein with possible exonuclease activity and involvement in DNA or RNA editing.

About this Structure

1V96 is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

Reference

Structure of PIN-domain protein PH0500 from Pyrococcus horikoshii., Jeyakanthan J, Inagaki E, Kuroishi C, Tahirov TH, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt, 5):463-8. Epub 2005 Apr 26. PMID:16511069

Page seeded by OCA on Mon Mar 31 00:21:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools