Structure of PDB 5uxe Chain B

Receptor sequence

>5uxeB (length=346) Species: 1502 (Clostridium perfringens)

AMARILKTAYTFDDVLLVPNKSEVLPNEVSLKTQLTKKIQLNIPLMSASM
DTVTESKMAIAMAREGGIGIIHKNMTIEDQAREVDRVKRSGGLLCGASIG
VTNDMMERVDAVVKAKVDVIVLDTAHGHSKGVIEGVKRIKAKYPELQVIA
GNIATPEAVRDLAEAGADCVKVGIGPGSICTTRIVAGVGVPQLTAVMDCA
EEGKKLGIPVIADGGLKYSGDIVKALAAGACAAMMGSIFAGCEEAPGAIE
IYQGRSYKVYRGMGSLGAMAKFVPEGVEGRIAYKGHLADTIYQLIGGIKS
GMGYLGAPTLENLYENANFVVQTSAGFRESHPHDINITKEAPNYSV

3D structure

• PDB: 5uxe Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens Complexed with IMP and P178
• Chain: B
• Resolution: 2.1 Å

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 M358 G359 S360 Y383 G385 M386 G387 E411	M50 G177 S178 I179 C180 D213 G215 M235 G236 S237 Y260 G262 M263 G264 E275
BS02	8LA	B	T247 A248 H249 S252 G254 M386 G387 M392 E411	T124 A125 H126 S129 G131 M263 G264 M269 E275
BS03	8LA	B	L24 P25 S436 G439 Y440	L25 P26 S300 G303 Y304

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

External links

• PDB: RCSB:5uxe, PDBe:5uxe, PDBj:5uxe
• PDBsum: 5uxe
• UniProt: A0A127ELD1