Structure of PDB 7rfh Chain E

Receptor sequence
>7rfhE (length=449) Species: 9606 (Homo sapiens) [Search protein sequence]
HETAAQRYSARLLQAGYMADYLISGGTGYVPEDGLTAQQLFASADGLTYN
DFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMA
LMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEA
KMRHGFSGIPITETGTLVGIVTSRDIDFLLLSEVMTPRIELVVAPAGVTL
KEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQL
LCGAAVGTREDDKYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKY
PHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCVMACGRPQGTAVYKVAE
YARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGSIQK
FVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVH
3D structure
PDB7rfh IMPDH1 retinal variants control filament architecture to tune allosteric regulation.
ChainE
Resolution3.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.205: IMP dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ATP E I157 T159 R161 D162 E184 L185 K206 G207 I170 T172 R174 D175 E190 L191 K212 G213
BS02 ATP E I115 P118 V119 F139 G141 K208 A223 T225 D226 I132 P135 V136 F156 G158 K214 A229 T231 D232
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:7rfh, PDBe:7rfh, PDBj:7rfh
PDBsum7rfh
PubMed35013599
UniProtP20839|IMDH1_HUMAN Inosine-5'-monophosphate dehydrogenase 1 (Gene Name=IMPDH1)

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