1mx5: Difference between revisions

Revision as of 02:10, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1mx5.png

1mx5, resolution 2.80Å ()

Ligands:

, , , ,

Activity:

Carboxylesterase, with EC number 3.1.1.1

Related:

1mx1, 1mx9

Structural annotation:
Resources:	CATH : 1Mx5A00, 1Mx5B00, 1Mx5C00, 1Mx5D00, 1Mx5E00, 1Mx5F00 InterPro : Ipr002018 Pfam : PF00135 SCOP : d1mx5a_, d1mx5b_, d1mx5c_, d1mx5d_, d1mx5e_, d1mx5f_ UniProt : P23141

Functional annotation:
Cellular component:	endoplasmic reticulum extracellular space
Biological process:	response to toxin metabolic process
Molecular function:	carboxylesterase activity hydrolase activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

Crystal Structure of Human Liver Carboxylesterase in complexed with homatropine, a cocaine analogueCrystal Structure of Human Liver Carboxylesterase in complexed with homatropine, a cocaine analogue

Template:ABSTRACT PUBMED 12679808

About this StructureAbout this Structure

1MX5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme., Bencharit S, Morton CL, Xue Y, Potter PM, Redinbo MR, Nat Struct Biol. 2003 May;10(5):349-56. PMID:12679808

Page seeded by OCA on Tue Jul 29 02:10:18 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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+===Crystal Structure of Human Liver Carboxylesterase in complexed with homatropine, a cocaine analogue===
-==Overview==
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-We present the first crystal structures of a human protein bound to analogs of cocaine and heroin. Human carboxylesterase 1 (hCE1) is a broad-spectrum bioscavenger that catalyzes the hydrolysis of heroin and cocaine, and the detoxification of organophosphate chemical weapons, such as sarin, soman and tabun. Crystal structures of the hCE1 glycoprotein in complex with the cocaine analog homatropine and the heroin analog naloxone provide explicit details about narcotic metabolism in humans. The hCE1 active site contains both specific and promiscuous compartments, which enable the enzyme to act on structurally distinct chemicals. A selective surface ligand-binding site regulates the trimer-hexamer equilibrium of hCE1 and allows each hCE1 monomer to bind two narcotic molecules simultaneously. The bioscavenger properties of hCE1 can likely be used to treat both narcotic overdose and chemical weapon exposure.
+The line below this paragraph, {{ABSTRACT_PUBMED_12679808}}, adds the Publication Abstract to the page
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 [[Category: Esterase]]
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