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2H0E

Crystal Structure of PucM in the absence of substrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0006144biological_processpurine nucleobase metabolic process
A0016787molecular_functionhydrolase activity
A0019628biological_processurate catabolic process
A0033971molecular_functionhydroxyisourate hydrolase activity
A0042802molecular_functionidentical protein binding
B0006144biological_processpurine nucleobase metabolic process
B0016787molecular_functionhydrolase activity
B0019628biological_processurate catabolic process
B0033971molecular_functionhydroxyisourate hydrolase activity
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 200
ChainResidue
AHIS14
AHIS14
AARG49
ATYR118
ATYR118
ASER121

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 201
ChainResidue
BARG49
BHIS105
BSER121

Functional Information from PROSITE/UniProt
site_idPS00768
Number of Residues16
DetailsTRANSTHYRETIN_1 Transthyretin signature 1. HILDltcGkPAanVkI
ChainResidueDetails
AHIS14-ILE29

site_idPS00769
Number of Residues13
DetailsTRANSTHYRETIN_2 Transthyretin signature 2. YHIPllLSPFGYQ
ChainResidueDetails
ATYR104-GLN116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AHIS14
AARG49
ATYR118
BHIS14
BARG49
BTYR118

225158

PDB entries from 2024-09-18

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