Structure of PDB 5uzs Chain B

Receptor sequence
>5uzsB (length=345) Species: 195103 (Clostridium perfringens ATCC 13124) [Search protein sequence]
SNAMARILKTAYTFDDVLLVPNKSEVLPNEVSLKTQLTKKIQLNIPLMSA
SMDTVTESKMAIAMAREGGIGIIHKNMTIEDQAREVDRVKRSGGLLCGAS
IGVTNDMMERVDAVVKAKVDVIVLDTAHGHSKGVIEGVKRIKAKYPELQV
IAGNIATPEAVRDLAEAGADCVKVGIGPGSICTTRIVAGVGVPQLTAVMD
CAEEGKKLGIPVIADGGLKYSGDIVKALAAGACAAMMGSIFAGCEEAPGA
IEIYQGRSYKVYRGMGSLGAMAFVPEGVEGRIAYKGHLADTIYQLIGGIK
SGMGYLGAPTLENLYENANFVVQTSAGFRESHPHDINITKEAPNY
3D structure
PDB5uzs Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens Complexed with IMP and P200
ChainB
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 IMP B M49 G300 S301 I302 C303 D336 G338 S360 Y383 G385 M386 G387 E411 M52 G179 S180 I181 C182 D215 G217 S239 Y262 G264 M265 G266 E276
BS02 8L4 B A248 H249 M386 G387 M392 E411 A127 H128 M265 G266 M271 E276
BS03 MG B E366 H422 E245 H287
BS04 8L4 B P25 S436 G439 Y440 P28 S301 G304 Y305
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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