Structure of PDB 7rgq Chain F

Receptor sequence
>7rgqF (length=481) Species: 9606 (Homo sapiens) [Search protein sequence]
GYVPEDGLTAQQLFASADGLTYNDFLILPGFIDFIADEVDLTSALTRKIT
LKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKF
EQGFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTS
RDIDFDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVND
CDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLT
QAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLI
DAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPIIAD
GGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGM
GSLKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMY
SGELKFEKRTMSAQIEGGVHGLHSYTFLPFT
3D structure
PDB7rgq IMPDH1 retinal variants control filament architecture to tune allosteric regulation.
ChainF
Resolution3.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.205: IMP dehydrogenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0003677 DNA binding
GO:0003723 RNA binding
GO:0003824 catalytic activity
GO:0003938 IMP dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006177 GMP biosynthetic process
GO:0006183 GTP biosynthetic process
Cellular Component
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0034774 secretory granule lumen
GO:0035578 azurophil granule lumen
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7rgq, PDBe:7rgq, PDBj:7rgq
PDBsum7rgq
PubMed35013599
UniProtP20839|IMDH1_HUMAN Inosine-5'-monophosphate dehydrogenase 1 (Gene Name=IMPDH1)

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