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1dku
From Proteopedia
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[[Image:1dku.png|left|200px]] | [[Image:1dku.png|left|200px]] | ||
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{{STRUCTURE_1dku| PDB=1dku | SCENE= }} | {{STRUCTURE_1dku| PDB=1dku | SCENE= }} | ||
===CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.=== | ===CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.=== | ||
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| - | (as it appears on PubMed at http://www.pubmed.gov), where 10742175 is the PubMed ID number. | ||
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{{ABSTRACT_PUBMED_10742175}} | {{ABSTRACT_PUBMED_10742175}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[1dku]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DKU OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:010742175</ref><references group="xtra"/> |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Ribose-phosphate diphosphokinase]] | [[Category: Ribose-phosphate diphosphokinase]] | ||
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[[Category: Open alpha-beta structure]] | [[Category: Open alpha-beta structure]] | ||
[[Category: Phosphoribosyltransferase type i fold]] | [[Category: Phosphoribosyltransferase type i fold]] | ||
| - | + | [[Category: Transferase]] | |
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Revision as of 09:53, 31 October 2012
CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.
Template:ABSTRACT PUBMED 10742175
About this Structure
1dku is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
- Eriksen TA, Kadziola A, Bentsen AK, Harlow KW, Larsen S. Structural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase. Nat Struct Biol. 2000 Apr;7(4):303-8. PMID:10742175 doi:10.1038/74069
