Cephalosporin acylase
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
- | <scene name='52/525143/Cv/2'>CSA contains 2 non-identical subunits</scene>. The <scene name='52/525143/Cv/3'>active site pocket</scene> of CSA is similar to that of penicillin acylase. CSA precursor is cleaved at 2 sites forming the active heterodimer. | + | <scene name='52/525143/Cv/2'>CSA contains 2 non-identical subunits</scene>. The <scene name='52/525143/Cv/3'>active site pocket</scene> (PDB entry [[1jw0]])<ref>PMID:11755403</ref> of CSA is similar to that of penicillin acylase. CSA precursor is cleaved at 2 sites forming the active heterodimer. |
</StructureSection> | </StructureSection> |
Revision as of 12:30, 13 December 2015
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3D structures of cephalosporin acylase
Updated on 13-December-2015
References
- ↑ Kim Y, Yoon K, Khang Y, Turley S, Hol WG. The 2.0 A crystal structure of cephalosporin acylase. Structure. 2000 Oct 15;8(10):1059-68. PMID:11080627
- ↑ Kim Y, Hol WG. Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity. Chem Biol. 2001 Dec;8(12):1253-64. PMID:11755403