1czf: Difference between revisions
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[[Image:1czf.png|left|200px]] | [[Image:1czf.png|left|200px]] | ||
{{STRUCTURE_1czf| PDB=1czf | SCENE= }} | {{STRUCTURE_1czf| PDB=1czf | SCENE= }} | ||
===ENDO-POLYGALACTURONASE II FROM ASPERGILLUS NIGER=== | ===ENDO-POLYGALACTURONASE II FROM ASPERGILLUS NIGER=== | ||
{{ABSTRACT_PUBMED_10521427}} | {{ABSTRACT_PUBMED_10521427}} | ||
==About this Structure== | ==About this Structure== | ||
[[1czf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CZF OCA]. | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:010521427</ref><ref group="xtra">PMID:011880627</ref><references group="xtra"/> | ||
[[Category: Aspergillus niger]] | [[Category: Aspergillus niger]] | ||
[[Category: Polygalacturonase]] | [[Category: Polygalacturonase]] | ||
Line 30: | Line 18: | ||
[[Category: Santen, Y van.]] | [[Category: Santen, Y van.]] | ||
[[Category: Beta helix]] | [[Category: Beta helix]] | ||
[[Category: Hydrolase]] | |||
Revision as of 23:03, 21 October 2012

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1czf, resolution 1.68Å () | |||||||||
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Ligands: | , | ||||||||
Activity: | Polygalacturonase, with EC number 3.2.1.15 | ||||||||
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Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
Coordinates: | save as pdb, mmCIF, xml |
ENDO-POLYGALACTURONASE II FROM ASPERGILLUS NIGERENDO-POLYGALACTURONASE II FROM ASPERGILLUS NIGER
Template:ABSTRACT PUBMED 10521427
About this StructureAbout this Structure
1czf is a 2 chain structure with sequence from Aspergillus niger. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ van Santen Y, Benen JA, Schroter KH, Kalk KH, Armand S, Visser J, Dijkstra BW. 1.68-A crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis. J Biol Chem. 1999 Oct 22;274(43):30474-80. PMID:10521427
- ↑ Richardson JS, Richardson DC. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2754-9. PMID:11880627 doi:10.1073/pnas.052706099