1cpx: Difference between revisions
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[[Image:1cpx.jpg|left|200px]] | [[Image:1cpx.jpg|left|200px]] | ||
'''BETA FORM OF CARBOXYPEPTIDASE A (RESIDUES 3-307) FROM BOVINE PANCREAS IN AN ORTHORHOMBIC CRYSTAL FORM WITH TWO ZINC IONS IN THE ACTIVE SITE.''' | {{Structure | ||
|PDB= 1cpx |SIZE=350|CAPTION= <scene name='initialview01'>1cpx</scene>, resolution 2.00Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=OH:HYDROXIDE ION'>OH</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Carboxypeptidase_A Carboxypeptidase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.1 3.4.17.1] | |||
|GENE= | |||
}} | |||
'''BETA FORM OF CARBOXYPEPTIDASE A (RESIDUES 3-307) FROM BOVINE PANCREAS IN AN ORTHORHOMBIC CRYSTAL FORM WITH TWO ZINC IONS IN THE ACTIVE SITE.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CPX is a [ | 1CPX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CPX OCA]. | ||
==Reference== | ==Reference== | ||
Native carboxypeptidase A in a new crystal environment reveals a different conformation of the important tyrosine 248., Bukrinsky JT, Bjerrum MJ, Kadziola A, Biochemistry. 1998 Nov 24;37(47):16555-64. PMID:[http:// | Native carboxypeptidase A in a new crystal environment reveals a different conformation of the important tyrosine 248., Bukrinsky JT, Bjerrum MJ, Kadziola A, Biochemistry. 1998 Nov 24;37(47):16555-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9843422 9843422] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Carboxypeptidase A]] | [[Category: Carboxypeptidase A]] | ||
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[[Category: zinc inhibition]] | [[Category: zinc inhibition]] | ||
''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 10:27:24 2008'' | ||
Revision as of 11:27, 20 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Carboxypeptidase A, with EC number 3.4.17.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BETA FORM OF CARBOXYPEPTIDASE A (RESIDUES 3-307) FROM BOVINE PANCREAS IN AN ORTHORHOMBIC CRYSTAL FORM WITH TWO ZINC IONS IN THE ACTIVE SITE.
OverviewOverview
Native carboxypeptidase A has been crystallized in a new crystal form, and the structure has been refined with X-ray data to 2.0 A resolution. In contrast to the previously published structure [Rees, D. C., Lewis, M., and Lipscomb, W. N. (1983) J. Mol. Biol. 168, 367-387], no active-site amino acids are involved in the crystal packing. The important Tyr248 is stabilized inside the active site by a hydrogen bond and by interactions with Ile247. The proposed role of Tyr248 in the induced fit mechanism is therefore not supported by the findings in this structure of native carboxypeptidase A. The structure has a partly populated inhibitory Zn2+ site in close proximity to the catalytic Zn2+ as evident from X-ray anomalous dispersion data. A hydroxo bridge is found between the catalytic Zn2+ and the inhibitory Zn2+ with a Zn2+-Zn2+ distance of 3.48 A. In addition, the inhibitory Zn2+ has Glu270 as a monodentate ligand. No other protein ligands to the inhibitory Zn2+ are seen. The crystals were grown at 0.3 M LiCl and weak evidence for a binding site for partly competitive inhibitory anions is observed.
About this StructureAbout this Structure
1CPX is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Native carboxypeptidase A in a new crystal environment reveals a different conformation of the important tyrosine 248., Bukrinsky JT, Bjerrum MJ, Kadziola A, Biochemistry. 1998 Nov 24;37(47):16555-64. PMID:9843422
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