4er1: Difference between revisions
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[[Image:4er1.jpg|left|200px]] | [[Image:4er1.jpg|left|200px]] | ||
'''THE ACTIVE SITE OF ASPARTIC PROTEINASES''' | {{Structure | ||
|PDB= 4er1 |SIZE=350|CAPTION= <scene name='initialview01'>4er1</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30] | |||
|GENE= | |||
}} | |||
'''THE ACTIVE SITE OF ASPARTIC PROTEINASES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
4ER1 is a [ | 4ER1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ER1 OCA]. | ||
==Reference== | ==Reference== | ||
The active site of aspartic proteinases., Pearl L, Blundell T, FEBS Lett. 1984 Aug 20;174(1):96-101. PMID:[http:// | The active site of aspartic proteinases., Pearl L, Blundell T, FEBS Lett. 1984 Aug 20;174(1):96-101. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/6381096 6381096] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase (acid proteinase)]] | [[Category: hydrolase (acid proteinase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:09:36 2008'' | ||
Revision as of 17:09, 20 March 2008
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| 4er1, resolution 2.0Å | |||||||||||||
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| Activity: | Hydrolase, with EC number 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
THE ACTIVE SITE OF ASPARTIC PROTEINASES
Overview
The active site of the aspartic proteinase, endothiapepsin, has been defined by X-ray analysis and restrained least-squares refinement at 2.1 A resolution with a crystallographic agreement value of 0.16. The environments of the two catalytically important aspartyl groups are remarkably similar and the contributions of the NH2- and COOH-terminal domains to the catalytic centre are related by a local 2-fold axis. The carboxylates of the aspartyls share a hydrogen bond and have equivalent contacts to a bound water molecule or hydroxonium ion lying on the local diad. The main chains around 32 and 215 are connected by a novel interaction involving diad-related threonines. It is suggested that the two pKa values of the active site aspartyls arise from a structure not unlike that in maleic acid with a hydrogen-bonded intermediate species and a dicarboxylate characterised by electrostatic repulsions between the two negatively charged groups.
About this Structure
4ER1 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
The active site of aspartic proteinases., Pearl L, Blundell T, FEBS Lett. 1984 Aug 20;174(1):96-101. PMID:6381096
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