2H1X

Crystal structure of 5-hydroxyisourate Hydrolase (formerly known as TRP, Transthyretin Related Protein)

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Functional Information from GO Data

ChainGOidnamespacecontents
A0005777cellular_componentperoxisome
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0033971molecular_functionhydroxyisourate hydrolase activity
A0006144biological_processpurine nucleobase metabolic process
A0019628biological_processurate catabolic process
B0005777cellular_componentperoxisome
B0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
B0033971molecular_functionhydroxyisourate hydrolase activity
B0006144biological_processpurine nucleobase metabolic process
B0019628biological_processurate catabolic process
C0005777cellular_componentperoxisome
C0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
C0033971molecular_functionhydroxyisourate hydrolase activity
C0006144biological_processpurine nucleobase metabolic process
C0019628biological_processurate catabolic process
D0005777cellular_componentperoxisome
D0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
D0033971molecular_functionhydroxyisourate hydrolase activity
D0006144biological_processpurine nucleobase metabolic process
D0019628biological_processurate catabolic process
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
PS0076864Transthyretin signature 1. [KH]-[IV]-L-[DN]-x(3)-G-x-P-[AG]-x(2)-[LIVM]-x-[IV]
ChainResidueDetails
AHIS12-ILE27
BHIS12-ILE27
CHIS12-ILE27
DHIS12-ILE27

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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
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Catalytic Information from CSA

site_idNumber of ResiduesDetails