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2DPL

Crystal Structure of the GMP synthase from Pyrococcus horikoshii OT3

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003921molecular_functionGMP synthase activity
A0003922molecular_functionGMP synthase (glutamine-hydrolyzing) activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0016874molecular_functionligase activity
A0046037biological_processGMP metabolic process
B0000166molecular_functionnucleotide binding
B0003921molecular_functionGMP synthase activity
B0003922molecular_functionGMP synthase (glutamine-hydrolyzing) activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006177biological_processGMP biosynthetic process
B0016874molecular_functionligase activity
B0046037biological_processGMP metabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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