3mla
From Proteopedia
(Difference between revisions)
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{{STRUCTURE_3mla| PDB=3mla | SCENE= }} | {{STRUCTURE_3mla| PDB=3mla | SCENE= }} | ||
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===BaNadD in complex with inhibitor 1_02=== | ===BaNadD in complex with inhibitor 1_02=== | ||
+ | {{ABSTRACT_PUBMED_020578699}} | ||
+ | ==Function== | ||
+ | [[http://www.uniprot.org/uniprot/NADD_BACAC NADD_BACAC]] Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD) (By similarity). | ||
==About this Structure== | ==About this Structure== | ||
- | + | [[3mla]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MLA OCA]. | |
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+ | ==Reference== | ||
+ | <ref group="xtra">PMID:020578699</ref><references group="xtra"/><references/> | ||
[[Category: Bacillus anthracis]] | [[Category: Bacillus anthracis]] | ||
[[Category: Nicotinate-nucleotide adenylyltransferase]] | [[Category: Nicotinate-nucleotide adenylyltransferase]] | ||
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[[Category: Nmnat-inhibitor complex]] | [[Category: Nmnat-inhibitor complex]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 28 12:39:04 2010'' |
Revision as of 21:06, 17 April 2013
Contents |
BaNadD in complex with inhibitor 1_02
Template:ABSTRACT PUBMED 020578699
Function
[NADD_BACAC] Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD) (By similarity).
About this Structure
3mla is a 2 chain structure with sequence from Bacillus anthracis. Full crystallographic information is available from OCA.
Reference
- Huang N, Kolhatkar R, Eyobo Y, Sorci L, Rodionova I, Osterman AL, Mackerell AD, Zhang H. Complexes of bacterial nicotinate mononucleotide adenylyltransferase with inhibitors: implication for structure-based drug design and improvement. J Med Chem. 2010 Jul 22;53(14):5229-39. PMID:20578699 doi:10.1021/jm100377f