2trm: Difference between revisions
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|PDB= 2trm |SIZE=350|CAPTION= <scene name='initialview01'>2trm</scene>, resolution 2.8Å | |PDB= 2trm |SIZE=350|CAPTION= <scene name='initialview01'>2trm</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2trm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2trm OCA], [http://www.ebi.ac.uk/pdbsum/2trm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2trm RCSB]</span> | |||
}} | }} | ||
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[[Category: Finer-Moore, J.]] | [[Category: Finer-Moore, J.]] | ||
[[Category: Stroud, R M.]] | [[Category: Stroud, R M.]] | ||
[[Category: hydrolase (serine proteinase)]] | [[Category: hydrolase (serine proteinase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:04:11 2008'' | ||
Revision as of 05:04, 31 March 2008
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| , resolution 2.8Å | |||||||
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| Ligands: | , | ||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS
OverviewOverview
The structure of the Asn102 mutant of trypsin was determined in order to distinguish whether the reduced activity of the mutant at neutral pH results from an altered active site conformation or from an inability to stabilize a positive charge on the active site histidine. The active site structure of the Asn102 mutant of trypsin is identical to the native enzyme with respect to the specificity pocket, the oxyanion hole, and the orientation of the nucleophilic serine. The observed decrease in rate results from the loss of nucleophilicity of the active site serine. This decreased nucleophilicity may result from stabilization of a His57 tautomer that is unable to accept the serine hydroxyl proton.
About this StructureAbout this Structure
2TRM is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis., Sprang S, Standing T, Fletterick RJ, Stroud RM, Finer-Moore J, Xuong NH, Hamlin R, Rutter WJ, Craik CS, Science. 1987 Aug 21;237(4817):905-9. PMID:3112942
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