2ex6
From Proteopedia
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===Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with ampicillin=== | ===Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with ampicillin=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[2ex6]] is a 1 chain structure of [[Penicillin-binding protein]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EX6 OCA]. | |
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| + | ==See Also== | ||
| + | *[[Penicillin-binding protein|Penicillin-binding protein]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:016411754</ref><references group="xtra"/> |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Kishida, H.]] | [[Category: Kishida, H.]] | ||
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[[Category: D-alanyl-d-alanine-carboxypeptidase]] | [[Category: D-alanyl-d-alanine-carboxypeptidase]] | ||
[[Category: D-alanyl-d-alanine-endopeptidase]] | [[Category: D-alanyl-d-alanine-endopeptidase]] | ||
| + | [[Category: Hydrolase]] | ||
[[Category: Penem]] | [[Category: Penem]] | ||
[[Category: Penicillin-binding protein]] | [[Category: Penicillin-binding protein]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 13:45:25 2009'' | ||
Revision as of 18:50, 26 July 2012
Contents |
Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with ampicillin
Template:ABSTRACT PUBMED 16411754
About this Structure
2ex6 is a 1 chain structure of Penicillin-binding protein with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Kishida H, Unzai S, Roper DI, Lloyd A, Park SY, Tame JR. Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics. Biochemistry. 2006 Jan 24;45(3):783-92. PMID:16411754 doi:10.1021/bi051533t
