2pec
From Proteopedia
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[[Image:2pec.png|left|200px]] | [[Image:2pec.png|left|200px]] | ||
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{{STRUCTURE_2pec| PDB=2pec | SCENE= }} | {{STRUCTURE_2pec| PDB=2pec | SCENE= }} | ||
===THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM=== | ===THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM=== | ||
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- | (as it appears on PubMed at http://www.pubmed.gov), where 7896002 is the PubMed ID number. | ||
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{{ABSTRACT_PUBMED_7896002}} | {{ABSTRACT_PUBMED_7896002}} | ||
==About this Structure== | ==About this Structure== | ||
- | + | [[2pec]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1pec 1pec]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PEC OCA]. | |
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:007896002</ref><ref group="xtra">PMID:011880627</ref><references group="xtra"/> |
[[Category: Erwinia chrysanthemi]] | [[Category: Erwinia chrysanthemi]] | ||
[[Category: Pectate lyase]] | [[Category: Pectate lyase]] | ||
[[Category: Jurnak, F.]] | [[Category: Jurnak, F.]] | ||
[[Category: Yoder, M D.]] | [[Category: Yoder, M D.]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:02:20 2009'' |
Revision as of 11:44, 7 January 2013
THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM
Template:ABSTRACT PUBMED 7896002
About this Structure
2pec is a 1 chain structure with sequence from Erwinia chrysanthemi. This structure supersedes the now removed PDB entry 1pec. Full crystallographic information is available from OCA.
Reference
- Yoder MD, Jurnak F. Protein motifs. 3. The parallel beta helix and other coiled folds. FASEB J. 1995 Mar;9(5):335-42. PMID:7896002
- 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