Structure of PDB 4q32 Chain C

Receptor sequence
>4q32C (length=341) Species: 195103 (Clostridium perfringens ATCC 13124) [Search protein sequence]
ILKTAYTFDDVLLVPNKSEVLPNEVSLKTQLTKKIQLNIPLMSASMDTVT
ESKMAIAMAREGGIGIIHKNMTIEDQAREVDRVKRSGGLLCGASIGVTND
MMERVDAVVKAKVDVIVLDTAHGHSKGVIEGVKRIKAKYPELQVIAGNIA
TPEAVRDLAEAGADCVKVGIGPGSICTTRIVAGVGVPQLTAVMDCAEEGK
KLGIPVIADGGLKYSGDIVKALAAGACAAMMGSIFAGCEEAPGAIEIYQG
RSYKVYRGMGSLGAMAKFVPEGVEGRIAYKGHLADTIYQLIGGIKSGMGY
LGAPTLENLYENANFVVQTSAGFRESHPHDINITKEAPNYS
3D structure
PDB4q32 Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens Complexed with IMP and C91
ChainC
Resolution2.788 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 C91 C S312 G315 S296 G299
BS02 IMP C M49 G176 S177 I178 C179 D212 G214 M234 G235 S236 Y259 G261 M262 G263 E287 M46 G173 S174 I175 C176 D209 G211 M231 G232 S233 Y256 G258 M259 G260 E271
BS03 C91 C A124 H125 M268 E287 A121 H122 M265 E271
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003938 IMP dehydrogenase activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4q32, PDBe:4q32, PDBj:4q32
PDBsum4q32
PubMed
UniProtA0A0H2YRZ7

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