1m35

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[[Image:1m35.gif|left|200px]]
[[Image:1m35.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1m35 |SIZE=350|CAPTION= <scene name='initialview01'>1m35</scene>, resolution 2.40&Aring;
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The line below this paragraph, containing "STRUCTURE_1m35", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= pepP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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-->
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|DOMAIN=
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{{STRUCTURE_1m35| PDB=1m35 | SCENE= }}
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|RELATEDENTRY=[[1az9|1AZ9]], [[1a16|1A16]], [[1jaw|1JAW]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m35 OCA], [http://www.ebi.ac.uk/pdbsum/1m35 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m35 RCSB]</span>
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}}
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'''Aminopeptidase P from Escherichia coli'''
'''Aminopeptidase P from Escherichia coli'''
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[[Category: Guss, J M.]]
[[Category: Guss, J M.]]
[[Category: Lee, M.]]
[[Category: Lee, M.]]
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[[Category: aminopeptidase]]
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[[Category: Aminopeptidase]]
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[[Category: manganese enzyme]]
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[[Category: Manganese enzyme]]
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[[Category: proline specific]]
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[[Category: Proline specific]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:34:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:10:39 2008''
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Revision as of 21:34, 2 May 2008

Image:1m35.gif

Template:STRUCTURE 1m35

Aminopeptidase P from Escherichia coli


Overview

Aminopeptidase P (AMPP) from Escherichia coli cleaves the N-terminal residue from an oligopeptide if the second residue is proline. The active site contains a dinuclear metal centre. Following earlier structural analyses of crystals in space groups P6(4)22 and I4(1)22, the structure of AMPP has been solved and refined in the orthorhombic space group C222(1) at 2.4 A resolution. There are six subunits in the asymmetric unit. These are arranged in two types of tetramer. One tetramer comprises four crystallographically independent subunits, while the other comprises two pairs of subunits related by a crystallographic twofold axis. The final model of 20 994 protein atoms, 1618 water molecules and 12 metal atoms refined to residuals R = 0.195 and R(free) = 0.215. The molecular structure confirms most of the previously reported features, including the subunit-subunit interfaces in the tetramer and persistent disorder at some residues. The metal-ligand bond lengths at the active site suggest that one of the two Mn atoms is five-coordinate rather than six-coordinate.

About this Structure

1M35 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

An orthorhombic form of Escherichia coli aminopeptidase P at 2.4 A resolution., Graham SC, Lee M, Freeman HC, Guss JM, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):897-902. Epub 2003, Apr 25. PMID:12777807 Page seeded by OCA on Sat May 3 00:34:41 2008

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