1uo6

From Proteopedia

(Difference between revisions)

Revision as of 08:04, 28 March 2018

PORCINE PANCREATIC ELASTASE/Xe-COMPLEX

Structural highlights

1uo6 is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	1b0e, 1bma, 1btu, 1c1m, 1e34, 1e35, 1e36, 1e37, 1e38, 1eai, 1eas, 1eat, 1eau, 1ela, 1elb, 1elc, 1eld, 1ele, 1elf, 1elg, 1esa, 1esb, 1est, 1fle, 1fzz, 1gvk, 1gwa, 1h9l, 1hax, 1hay, 1haz, 1hb0, 1hv7, 1inc, 1jim, 1l0z, 1l1g, 1lka, 1lkb, 1lvy, 1mcv, 1mmj, 1nes, 1okx, 1qgf, 1qix, 1qnj, 1qr3, 2est, 3est, 4est, 5est, 6est, 7est, 8est, 9est
Activity:	Pancreatic elastase, with EC number 3.4.21.36
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CELA1_PIG] Acts upon elastin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Complete and highly redundant data sets were collected at nine different wavelengths between 0.80 and 2.65 A on a xenon derivative of porcine pancreatic elastase in both air and helium atmospheres. The magnitude of the anomalous signal, as assessed by the xenon-peak height in the anomalous difference Patterson synthesis, is affected by the wavelength of data collection as well as by the scaling model used. For data collected at wavelengths longer than 1.7 A, the use of a three-dimensional scaling protocol is essential in order to obtain the highest possible anomalous signal. Based on the scaling protocols currently available, the optimal wavelength range for data collection appears to be between 2.1 and 2.4 A. Beyond that, any further increase in signal will be compensated for or even superseded by a concomitant increase in noise, which cannot be fully corrected for. Data collection in a helium atmosphere yields higher I/sigma(I) values, but not significantly better anomalous differences, than data collection in air.

On the routine use of soft X-rays in macromolecular crystallography. Part II. Data-collection wavelength and scaling models.,Mueller-Dieckmann C, Polentarutti M, Djinovic Carugo K, Panjikar S, Tucker PA, Weiss MS Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):28-38. Epub 2003, Dec 18. PMID:14684889^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mueller-Dieckmann C, Polentarutti M, Djinovic Carugo K, Panjikar S, Tucker PA, Weiss MS. On the routine use of soft X-rays in macromolecular crystallography. Part II. Data-collection wavelength and scaling models. Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):28-38. Epub 2003, Dec 18. PMID:14684889

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uo6"

@@ Line 1: / Line 1: @@
-==PORCINE PANCREATIC ELASTASE/XE-COMPLEX==
+==PORCINE PANCREATIC ELASTASE/Xe-COMPLEX==
 <StructureSection load='1uo6' size='340' side='right' caption='[[1uo6]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b0e|1b0e]], [[1bma|1bma]], [[1btu|1btu]], [[1c1m|1c1m]], [[1e34|1e34]], [[1e35|1e35]], [[1e36|1e36]], [[1e37|1e37]], [[1e38|1e38]], [[1eai|1eai]], [[1eas|1eas]], [[1eat|1eat]], [[1eau|1eau]], [[1ela|1ela]], [[1elb|1elb]], [[1elc|1elc]], [[1eld|1eld]], [[1ele|1ele]], [[1elf|1elf]], [[1elg|1elg]], [[1esa|1esa]], [[1esb|1esb]], [[1est|1est]], [[1fle|1fle]], [[1fzz|1fzz]], [[1gvk|1gvk]], [[1gwa|1gwa]], [[1h9l|1h9l]], [[1hax|1hax]], [[1hay|1hay]], [[1haz|1haz]], [[1hb0|1hb0]], [[1hv7|1hv7]], [[1inc|1inc]], [[1jim|1jim]], [[1l0z|1l0z]], [[1l1g|1l1g]], [[1lka|1lka]], [[1lkb|1lkb]], [[1lvy|1lvy]], [[1mcv|1mcv]], [[1mmj|1mmj]], [[1nes|1nes]], [[1okx|1okx]], [[1qgf|1qgf]], [[1qix|1qix]], [[1qnj|1qnj]], [[1qr3|1qr3]], [[2est|2est]], [[3est|3est]], [[4est|4est]], [[5est|5est]], [[6est|6est]], [[7est|7est]], [[8est|8est]], [[9est|9est]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uo6 OCA], [http://pdbe.org/1uo6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uo6 RCSB], [http://www.ebi.ac.uk/pdbsum/1uo6 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uo6 OCA], [http://pdbe.org/1uo6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uo6 RCSB], [http://www.ebi.ac.uk/pdbsum/1uo6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uo6 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uo/1uo6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uo/1uo6_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1uo6 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1uo6

From Proteopedia

Revision as of 08:04, 28 March 2018

PORCINE PANCREATIC ELASTASE/Xe-COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox