4cfs: Difference between revisions
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{{STRUCTURE_4cfs| PDB=4cfs | SCENE= }} | {{STRUCTURE_4cfs| PDB=4cfs | SCENE= }} | ||
===CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4- OXOQUINALDINE 2,4-DIOXYGENASE (HOD) CATALYTICALLY INACTIVE H251A VARIANT COMPLEXED WITH ITS NATURAL SUBSTRATE 1-H-3-HYDROXY-4- OXOQUINALDINE=== | ===CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4- OXOQUINALDINE 2,4-DIOXYGENASE (HOD) CATALYTICALLY INACTIVE H251A VARIANT COMPLEXED WITH ITS NATURAL SUBSTRATE 1-H-3-HYDROXY-4- OXOQUINALDINE=== | ||
{{ | {{ABSTRACT_PUBMED_24482238}} | ||
==Function== | ==Function== | ||
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==About this Structure== | ==About this Structure== | ||
[[4cfs]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CFS OCA]. | [[4cfs]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Artnt Artnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CFS OCA]. | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:024482238</ref><references group="xtra"/><references/> | ||
[[Category: 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase]] | [[Category: 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase]] | ||
[[Category: Artnt]] | |||
[[Category: Bui, S.]] | [[Category: Bui, S.]] | ||
[[Category: Steiner, R A.]] | [[Category: Steiner, R A.]] | ||
Revision as of 03:31, 13 February 2014
CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4- OXOQUINALDINE 2,4-DIOXYGENASE (HOD) CATALYTICALLY INACTIVE H251A VARIANT COMPLEXED WITH ITS NATURAL SUBSTRATE 1-H-3-HYDROXY-4- OXOQUINALDINE
Template:ABSTRACT PUBMED 24482238
Function
[HOD_ARTNT] Ring-cleaving dioxygenase involved in quinaldine degradation and utilization.[1]
About this Structure
4cfs is a 4 chain structure with sequence from Artnt. Full crystallographic information is available from OCA.
Reference
- Hernandez-Ortega A, Quesne MG, Bui S, Heuts DP, Steiner RA, Heyes DJ, de Visser SP, Scrutton NS. Origin of the proton-transfer step in the cofactor-free 1-H-3-hydroxy-4-oxoquinaldine 2,4- dioxygenase: Effect of the basicity of an active site His residue. J Biol Chem. 2014 Jan 30. PMID:24482238 doi:https://dx.doi.org/10.1074/jbc.M113.543033
