Thioesterase: Difference between revisions

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<StructureSection load='2hd5' size='350' side='right' caption='Human ubiquitin esterase 2 (grey) complex with ubiquitin (green) and zinc+2 ion (grey) (PDB code [[2hd5]]).' scene=''>
<StructureSection load='2hd5' size='450' side='right' caption='Human ubiquitin esterase 2 (deepskyblue) complex with ubiquitin (green) and zinc+2 ion (grey) (PDB code [[2hd5]]).' scene='48/489265/Cv/2'>
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== Function ==
== Function ==
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== Structural highlights ==
== Structural highlights ==
Ubiquitin thioesterase 2 active site contains the catalytic triad Cys-His-Asn and the oxyanion hole Asn.  The metal-binding enzyme contains a Zn+2 ion which coordinates to 4 Cys residues.  The ubiquitin coordinates to the thioesterase via residues in all thioesterase domains: finger, palm and thumb<ref>PMID:16905103</ref>.
<scene name='48/489265/Cv/3'>Human ubiquitin esterase 2 complex with ubiquitin and zinc+2 ion</scene>. Ubiquitin thioesterase 2 active site contains the <scene name='48/489265/Cv/1'>catalytic triad Cys-His-Asn and the oxyanion hole Asn</scene>.  The metal-binding enzyme contains a Zn+2 ion which coordinates to 4 Cys residues.  The ubiquitin coordinates to the thioesterase via residues in all thioesterase domains: finger, palm and thumb<ref>PMID:16905103</ref>.
</StructureSection>
</StructureSection>
==3D structures of thioesterase==
==3D structures of thioesterase==

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Michal Harel, Alexander Berchansky, Joel L. Sussman