3c4p
From Proteopedia
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| - | [[Image:3c4p.png|left|200px]] | ||
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{{STRUCTURE_3c4p| PDB=3c4p | SCENE= }} | {{STRUCTURE_3c4p| PDB=3c4p | SCENE= }} | ||
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===Crystal Structure of the SHV-1 Beta-lactamase/Beta-lactamase inhibitor protein (BLIP) E73M complex=== | ===Crystal Structure of the SHV-1 Beta-lactamase/Beta-lactamase inhibitor protein (BLIP) E73M complex=== | ||
| + | {{ABSTRACT_PUBMED_18775544}} | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/BLIP_STRCL BLIP_STRCL]] Inhibits a wide variety of beta lactamases. | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:018775544</ref><references group="xtra"/> | + | <ref group="xtra">PMID:018775544</ref><references group="xtra"/><references/> |
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Klebsiella pneumoniae]] | [[Category: Klebsiella pneumoniae]] | ||
Revision as of 12:33, 3 July 2013
Contents |
Crystal Structure of the SHV-1 Beta-lactamase/Beta-lactamase inhibitor protein (BLIP) E73M complex
Template:ABSTRACT PUBMED 18775544
Function
[BLIP_STRCL] Inhibits a wide variety of beta lactamases.
About this Structure
3c4p is a 2 chain structure with sequence from Klebsiella pneumoniae and Streptomyces clavuligerus. Full crystallographic information is available from OCA.
See Also
Reference
- Reynolds KA, Hanes MS, Thomson JM, Antczak AJ, Berger JM, Bonomo RA, Kirsch JF, Handel TM. Computational redesign of the SHV-1 beta-lactamase/beta-lactamase inhibitor protein interface. J Mol Biol. 2008 Oct 24;382(5):1265-75. Epub 2008 May 29. PMID:18775544 doi:http://dx.doi.org/10.1016/j.jmb.2008.05.051
Categories: Beta-lactamase | Klebsiella pneumoniae | Streptomyces clavuligerus | Antczak, A J. | Berger, J M. | Bonomo, R A. | Handel, T M. | Hanes, M S. | Kirsch, J F. | Reynolds, K A. | Thomson, J M. | Antibiotic resistance | Beta-lactamase inhibitory protein | Blip | Hydrolase | Hydrolase-hydrolase inhibitor complex | Protein-protein complex | Secreted | Shv-1
