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1ceg
From Proteopedia
(Difference between revisions)
| Line 20: | Line 20: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1CEG is a | + | 1CEG is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEG OCA]. |
==Reference== | ==Reference== | ||
| - | + | <ref group="xtra">PMID:7626623</ref><references group="xtra"/> | |
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]] | [[Category: Serine-type D-Ala-D-Ala carboxypeptidase]] | ||
| - | [[Category: Single protein]] | ||
[[Category: Streptomyces sp.]] | [[Category: Streptomyces sp.]] | ||
[[Category: Knox, J R.]] | [[Category: Knox, J R.]] | ||
| Line 33: | Line 32: | ||
[[Category: Penicillin target]] | [[Category: Penicillin target]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:39:02 2009'' |
Revision as of 06:39, 18 February 2009
CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE
Template:ABSTRACT PUBMED 7626623
About this Structure
1CEG is a 1 chain structure of sequence from Streptomyces sp.. Full crystallographic information is available from OCA.
Reference
- Kuzin AP, Liu H, Kelly JA, Knox JR. Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases. Biochemistry. 1995 Jul 25;34(29):9532-40. PMID:7626623
Page seeded by OCA on Wed Feb 18 08:39:02 2009
