Structure of PDB 4q32 Chain A

Receptor sequence
>4q32A (length=337) Species: 195103 (Clostridium perfringens ATCC 13124) [Search protein sequence]
KTAYTFDDVLLVPNKSEVLPNEVSLKTQLTKKIQLNIPLMSASMDTVTES
KMAIAMAREGGIGIIHKNMTIEDQAREVDRVKRSGGLLCGASIGVTNDMM
ERVDAVVKAKVDVIVLDTAHGHSKGVIEGVKRIKAKYPELQVIAGNIATP
EAVRDLAEAGADCVKVGIGPGSICTTRIVAGVGVPQLTAVMDCAEEGKKL
GIPVIADGGLKYSGDIVKALAAGACAAMMGSIFAGCEEAPGAIEIYQGRS
YKVYRGMGSLGAMAVPEGVEGRIAYKGHLADTIYQLIGGIKSGMGYLGAP
TLENLYENANFVVQTSAGFRESHPHDINITKEAPNYS
3D structure
PDB4q32 Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens Complexed with IMP and C91
ChainA
Resolution2.788 Å
3D
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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 IMP A M49 G176 S177 I178 C179 D212 G213 G214 S236 G261 M262 G263 E287 M44 G171 S172 I173 C174 D207 G208 G209 S231 G256 M257 G258 E267
BS02 C91 A A124 M268 A119 M263
BS03 C91 A P25 G315 Y316 P20 G295 Y296
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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