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2D7J

Crystal Structure Analysis of Glutamine Amidotransferase 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
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues187
DetailsDomain: {"description":"Glutamine amidotransferase type-1","evidences":[{"source":"HAMAP-Rule","id":"MF_01510","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01510","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01510","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
ACYS79
AHIS166
AGLU168

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
ACYS79
AHIS166

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PDB entries from 2025-11-05

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