1igb

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|PDB= 1igb |SIZE=350|CAPTION= <scene name='initialview01'>1igb</scene>, resolution 2.3&Aring;
|PDB= 1igb |SIZE=350|CAPTION= <scene name='initialview01'>1igb</scene>, resolution 2.3&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=IPO:PARA-IODO-D-PHENYLALANINE HYDROXAMIC ACID'>IPO</scene>
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|LIGAND= <scene name='pdbligand=IPO:PARA-IODO-D-PHENYLALANINE+HYDROXAMIC+ACID'>IPO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1igb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1igb OCA], [http://www.ebi.ac.uk/pdbsum/1igb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1igb RCSB]</span>
}}
}}
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[[Category: Schalk, C.]]
[[Category: Schalk, C.]]
[[Category: Tarnus, C.]]
[[Category: Tarnus, C.]]
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[[Category: IPO]]
 
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[[Category: ZN]]
 
[[Category: aminopeptidase]]
[[Category: aminopeptidase]]
[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:50:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:19:22 2008''

Revision as of 18:19, 30 March 2008


PDB ID 1igb

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands: ,
Activity: Bacterial leucyl aminopeptidase, with EC number 3.4.11.10
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



AEROMONAS PROTEOLYTICA AMINOPEPTIDASE COMPLEXED WITH THE INHIBITOR PARA-IODO-D-PHENYLALANINE HYDROXAMATE


Overview

The structure of the complex of Aeromonas proteolytica aminopeptidase, a two-zinc exopeptidase, with the inhibitor p-iodo-D-phenylalanine hydroxamate has been determined by X-ray crystallography. Refinement of the structure, which includes 220 water molecules, using data at 0.80-0.23-nm resolution resulted in a crystallographic residual R value of 16%. The hydroxamate group adopts a planar conformation whereby the two oxygen atoms interact with the zinc ions. The N-hydroxyl group of the inhibitor is located between the two zinc ions, a position which is close to that occupied by a water molecule in the native structure. The carbonyl oxygen of the inhibitor binds to Zn1, which becomes pentacoordinated while Zn2 remains tetracoordinated, in contrast to the native protein where both zinc ions were shown to be tetracoordinated and structurally equivalent. Interactions of the carboxylate oxygens of Glu151 with the hydroxamate group play an important role in the stabilization of the complex.

About this Structure

1IGB is a Single protein structure of sequence from Vibrio proteolyticus. Full crystallographic information is available from OCA.

Reference

The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit., Chevrier B, D'Orchymont H, Schalk C, Tarnus C, Moras D, Eur J Biochem. 1996 Apr 15;237(2):393-8. PMID:8647077

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