2agg: Difference between revisions

Revision as of 07:05, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2agg.png

2agg, resolution 1.28Å ()

Ligands:

,

Non-Standard Residues:

Activity:

Trypsin, with EC number 3.4.21.4

Related:

2age, 2agi, 2ah4

Structural annotation:
Resources:	CATH : 2Aggx02, 2Aggx01 InterPro : Ipr001254, Ipr018114, Ipr009003, Ipr001314 Pfam : PF00089 SCOP : d2aggx1

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

succinyl-AAPK-trypsin acyl-enzyme at 1.28 A resolutionsuccinyl-AAPK-trypsin acyl-enzyme at 1.28 A resolution

Template:ABSTRACT PUBMED 16636277

About this StructureAbout this Structure

2AGG is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates., Radisky ES, Lee JM, Lu CJ, Koshland DE Jr, Proc Natl Acad Sci U S A. 2006 May 2;103(18):6835-40. Epub 2006 Apr 24. PMID:16636277

Page seeded by OCA on Mon Jul 28 07:05:01 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-==Overview==
+<!--
-Atomic resolution structures of trypsin acyl-enzymes and a tetrahedral intermediate analog, along with previously solved structures representing the Michaelis complex, are used to reconstruct events in the catalytic cycle of this classic serine protease. Structural comparisons provide insight into active site adjustments involved in catalysis. Subtle motions of the catalytic serine and histidine residues coordinated with translation of the substrate reaction center are seen to favor the forward progress of the acylation reaction. The structures also clarify the attack trajectory of the hydrolytic water in the deacylation reaction.
+The line below this paragraph, {{ABSTRACT_PUBMED_16636277}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16636277 is the PubMed ID number.
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 [[Category: Proteinase]]
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