4onw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "4onw" [edit=sysop:move=sysop])
Line 1: Line 1:
-
'''Unreleased structure'''
+
{{STRUCTURE_4onw| PDB=4onw | SCENE= }}
 +
===Crystal structure of the catalytic domain of DapE protein from V.cholerea===
-
The entry 4onw is ON HOLD
+
==Function==
 +
[[http://www.uniprot.org/uniprot/DAPE_VIBCH 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]
-
Authors: Nocek, B., Makowska-Grzyska, M., Jedrzejczak, R., Gu, M., Anderson, W.F., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)
+
==About this Structure==
-
 
+
[[4onw]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3t68 3t68]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ONW OCA].
-
Description: Crystal structure of the catalytic domain of DapE protein from V.cholerea
+
[[Category: Succinyl-diaminopimelate desuccinylase]]
 +
[[Category: Anderson, W F.]]
 +
[[Category: CSGID, Center for Structural Genomics of Infectious Diseases.]]
 +
[[Category: Gu, M.]]
 +
[[Category: Jedrzejczak, R.]]
 +
[[Category: Joachimiak, A.]]
 +
[[Category: Makowska-Grzyska, M.]]
 +
[[Category: Nocek, B.]]
 +
[[Category: Aminopeptidase]]
 +
[[Category: Center for structural genomics of infectious disease]]
 +
[[Category: Csgid]]
 +
[[Category: Dape]]
 +
[[Category: Hydrolase]]
 +
[[Category: M20]]
 +
[[Category: National institute of allergy and infectious disease]]
 +
[[Category: Niaid]]
 +
[[Category: Structural genomic]]
 +
[[Category: Zn binding]]

Revision as of 07:36, 23 April 2014

Template:STRUCTURE 4onw

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?)

OCA

Personal tools