Structure of PDB 5uzs Chain D

Receptor sequence
>5uzsD (length=347) Species: 195103 (Clostridium perfringens ATCC 13124) [Search protein sequence]
SNAMARILKTAYTFDDVLLVPNKSEVLPNEVSLKTQLTKKIQLNIPLMSA
SMDTVTESKMAIAMAREGGIGIIHKNMTIEDQAREVDRVKRSGGLLCGAS
IGVTNDMMERVDAVVKAKVDVIVLDTAHGHSKGVIEGVKRIKAKYPELQV
IAGNIATPEAVRDLAEAGADCVKVGIGPGSICTTRIVAGVGVPQLTAVMD
CAEEGKKLGIPVIADGGLKYSGDIVKALAAGACAAMMGSIFAGCEEAPGA
IEIYQGRSYKVYRGMGSLGAMAKFVPEGVEGRIAYKGHLADTIYQLIGGI
KSGMGYLGAPTLENLYENANFVVQTSAGFRESHPHDINITKEAPNYS
3D structure
PDB5uzs Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens Complexed with IMP and P200
ChainD
Resolution2.367 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 8L4 D P25 S436 G439 Y440 P28 S302 G305 Y306
BS02 IMP D M49 G300 S301 I302 C303 D336 G338 M358 G359 S360 Y383 G385 M386 G387 E411 M52 G179 S180 I181 C182 D215 G217 M237 G238 S239 Y262 G264 M265 G266 E277
BS03 8L4 D A248 H249 M386 G387 M392 E411 A127 H128 M265 G266 M271 E277
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:5uzs, PDBe:5uzs, PDBj:5uzs
PDBsum5uzs
PubMed
UniProtA0A0H2YRZ7

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