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8EBC

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Listeria monocytogenes in the complex with IMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0006164biological_processpurine nucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
B0003824molecular_functioncatalytic activity
B0003938molecular_functionIMP dehydrogenase activity
B0006164biological_processpurine nucleotide biosynthetic process
B0016491molecular_functionoxidoreductase activity
C0003824molecular_functioncatalytic activity
C0003938molecular_functionIMP dehydrogenase activity
C0006164biological_processpurine nucleotide biosynthetic process
C0016491molecular_functionoxidoreductase activity
D0003824molecular_functioncatalytic activity
D0003938molecular_functionIMP dehydrogenase activity
D0006164biological_processpurine nucleotide biosynthetic process
D0016491molecular_functionoxidoreductase activity
E0003824molecular_functioncatalytic activity
E0003938molecular_functionIMP dehydrogenase activity
E0006164biological_processpurine nucleotide biosynthetic process
E0016491molecular_functionoxidoreductase activity
F0003824molecular_functioncatalytic activity
F0003938molecular_functionIMP dehydrogenase activity
F0006164biological_processpurine nucleotide biosynthetic process
F0016491molecular_functionoxidoreductase activity
Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. VKVGVGgGSICiT
ChainResidueDetails
AVAL200-THR212

237735

PDB entries from 2025-06-18

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