2ex2: Difference between revisions
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{{STRUCTURE_2ex2| PDB=2ex2 | SCENE= }} | {{STRUCTURE_2ex2| PDB=2ex2 | SCENE= }} | ||
===Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli=== | ===Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli=== | ||
{{ABSTRACT_PUBMED_16411754}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/DACB_ECOLI DACB_ECOLI]] Not involved in transpeptidation but exclusively catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction.<ref>PMID:2046551</ref> | |||
==About this Structure== | ==About this Structure== | ||
[[2ex2]] is a 1 chain structure 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=2EX2 OCA]. | [[2ex2]] is a 1 chain structure 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=2EX2 OCA]. | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:016411754</ref><references group="xtra"/> | <ref group="xtra">PMID:016411754</ref><references group="xtra"/><references/> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Kishida, H.]] | [[Category: Kishida, H.]] | ||
Revision as of 08:01, 30 June 2013
Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli
Template:ABSTRACT PUBMED 16411754
Function
[DACB_ECOLI] Not involved in transpeptidation but exclusively catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction.[1]
About this Structure
2ex2 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
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
