1ac5
From Proteopedia
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|SITE= <scene name='pdbsite=176:Member+Of+Catalytic+Triad'>176</scene>, <scene name='pdbsite=383:Member+Of+Catalytic+Triad'>383</scene> and <scene name='pdbsite=448:Member+Of+Catalytic+Triad'>448</scene> | |SITE= <scene name='pdbsite=176:Member+Of+Catalytic+Triad'>176</scene>, <scene name='pdbsite=383:Member+Of+Catalytic+Triad'>383</scene> and <scene name='pdbsite=448:Member+Of+Catalytic+Triad'>448</scene> | ||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Carboxypeptidase_D Carboxypeptidase D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.6 3.4.16.6] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxypeptidase_D Carboxypeptidase D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.6 3.4.16.6] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ac5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ac5 OCA], [http://www.ebi.ac.uk/pdbsum/1ac5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ac5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Shilton, B H.]] | [[Category: Shilton, B H.]] | ||
[[Category: Thomas, D Y.]] | [[Category: Thomas, D Y.]] | ||
| - | [[Category: NAG]] | ||
[[Category: carboxypeptidase]] | [[Category: carboxypeptidase]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:37:25 2008'' |
Revision as of 15:37, 30 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | |||||||
| Activity: | Carboxypeptidase D, with EC number 3.4.16.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE
Overview
A soluble form of the killer factor and prohormone-processing carboxypeptidase, "Kex1 delta p," from Saccharomyces cerevisiae, has been crystallized in 17-22% poly(enthylene glycol) methyl ether (average M(r) = 5,000), 100 mM ammonium acetate, 5% glycerol, pH 6.5, at 20 degrees C. A native data set (2.8 A resolution) and four derivative data sets (3.0-3.2 A resolution) were collected at the Photon Factory (lambda = 1.0 A). The crystals belong to space group P2(1)2(1)2(1) with a =56.6 A, b = 84.0 A, c = 111.8 A. Freezing a Kex1 delta p crystal has facilitated the collection of a 2.4-A data set using a rotating anode source (lambda = 1.5418 A). Molecular replacement models have been built based on the structures of wheat serine carboxypeptidase (CPDW-II; Liao DI et al., 1992, Biochemistry 31:9796-9812) and yeast carboxypeptidase Y.
About this Structure
1AC5 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystallization of a soluble form of the Kex1p serine carboxypeptidase from Saccharomyces cerevisiae., Shilton BH, Li Y, Tessier D, Thomas DY, Cygler M, Protein Sci. 1996 Feb;5(2):395-7. PMID:8745419
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