This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1v0l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:06, 13 December 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='1v0l' size='340' side='right'caption='[[1v0l]], [[Resolution|resolution]] 0.98&Aring;' scene=''>
<StructureSection load='1v0l' size='340' side='right'caption='[[1v0l]], [[Resolution|resolution]] 0.98&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1v0l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V0L FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1v0l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V0L FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XIF:PIPERIDINE-3,4-DIOL'>XIF</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.98&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e0v|1e0v]], [[1e0w|1e0w]], [[1e0x|1e0x]], [[1knl|1knl]], [[1knm|1knm]], [[1mc9|1mc9]], [[1od8|1od8]], [[1v0k|1v0k]], [[1v0m|1v0m]], [[1v0n|1v0n]], [[1xas|1xas]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XIF:PIPERIDINE-3,4-DIOL'>XIF</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v0l OCA], [https://pdbe.org/1v0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v0l RCSB], [https://www.ebi.ac.uk/pdbsum/1v0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v0l ProSAT]</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=1v0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v0l OCA], [http://pdbe.org/1v0l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v0l RCSB], [http://www.ebi.ac.uk/pdbsum/1v0l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v0l ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/XYNA_STRLI XYNA_STRLI]] Contributes to hydrolyze hemicellulose, the major component of plant cell-walls. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources.
+
[https://www.uniprot.org/uniprot/XYNA_STRLI XYNA_STRLI] Contributes to hydrolyze hemicellulose, the major component of plant cell-walls. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 34: Line 33:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Actinomyces lividans krasil'nikov et al. 1965]]
 
-
[[Category: Endo-1,4-beta-xylanase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Davies, G J]]
+
[[Category: Streptomyces lividans]]
-
[[Category: Gloster, T M]]
+
[[Category: Davies GJ]]
-
[[Category: Roberts, S]]
+
[[Category: Gloster TM]]
-
[[Category: Tarling, C A]]
+
[[Category: Roberts S]]
-
[[Category: Wicki, J]]
+
[[Category: Tarling CA]]
-
[[Category: Williams, S J]]
+
[[Category: Wicki J]]
-
[[Category: Withers, S G]]
+
[[Category: Williams SJ]]
-
[[Category: Glycoside hydrolase family 10]]
+
[[Category: Withers SG]]
-
[[Category: Hydrolase]]
+
-
[[Category: Isofagomine]]
+
-
[[Category: Xylan degradation]]
+
-
[[Category: Xylanase]]
+

Current revision

Xylanase Xyn10A from Streptomyces lividans in complex with xylobio-isofagomine at pH 5.8

PDB ID 1v0l

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools