4onw | pdb_00004onw
From Proteopedia
Crystal structure of the catalytic domain of DapE protein from V.cholerea
Function
[DAPE_VIBCH] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls (By similarity).[HAMAP-Rule:MF_01690]
About this Structure
4onw is a 2 chain structure. This structure supersedes the now removed PDB entry 3t68. Full crystallographic information is available from OCA.
Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Succinyl-diaminopimelate desuccinylase
- Anderson, W F.
- CSGID, Center for Structural Genomics of Infectious Diseases.
- Gu, M.
- Jedrzejczak, R.
- Joachimiak, A.
- Makowska-Grzyska, M.
- Nocek, B.
- Aminopeptidase
- Center for structural genomics of infectious disease
- Csgid
- Dape
- Hydrolase
- M20
- National institute of allergy and infectious disease
- Niaid
- Structural genomic
- Zn binding
