4o23

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m (Protected "4o23" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4o23| PDB=4o23 | SCENE= }}
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===Crystal structure of mono-zinc form of succinyl diaminopimelate desuccinylase from Neisseria meningitidis MC58===
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The entry 4o23 is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/DAPE_NEIMB DAPE_NEIMB]] 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]
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Authors: Nocek, B., Holz, R., Anderson, W.F., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)
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==About this Structure==
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[[4o23]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O23 OCA].
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Description: Crystal structure of mono-zinc form of succinyl diaminopimelate desuccinylase from Neisseria meningitidis MC58
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[[Category: Succinyl-diaminopimelate desuccinylase]]
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[[Category: Anderson, W F.]]
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[[Category: CSGID, Center for Structural Genomics of Infectious Diseases.]]
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[[Category: Holz, R.]]
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[[Category: Joachimiak, A.]]
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[[Category: Nocek, B.]]
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[[Category: Center for structural genomics of infectious disease]]
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[[Category: Csgid]]
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[[Category: Dape]]
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[[Category: Hydrolase]]
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[[Category: Structural genomic]]

Revision as of 08:28, 15 January 2014

Template:STRUCTURE 4o23

Crystal structure of mono-zinc form of succinyl diaminopimelate desuccinylase from Neisseria meningitidis MC58

Function

[DAPE_NEIMB] 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

4o23 is a 2 chain structure. Full crystallographic information is available from OCA.

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