Structure of PDB 4q33 Chain F

Receptor sequence
>4q33F (length=344) Species: 195103 (Clostridium perfringens ATCC 13124) [Search protein sequence]
ARILKTAYTFDDVLLVPNKSEVLPNEVSLKTQLTKKIQLNIPLMSASMDT
VTESKMAIAMAREGGIGIIHKNMTIEDQAREVDRVKRSGGLLCGASIGVT
NDMMERVDAVVKAKVDVIVLDTAHGHSKGVIEGVKRIKAKYPELQVIAGN
IATPEAVRDLAEAGADCVKVGIGPGSICTTRIVAGVGVPQLTAVMDCAEE
GKKLGIPVIADGGLKYSGDIVKALAAGACAAMMGSIFAGCEEAPGAIEIY
QGRSYKVYRGMGSLGAMAKKFVPEGVEGRIAYKGHLADTIYQLIGGIKSG
MGYLGAPTLENLYENANFVVQTSAGFRESHPHDINITKEAPNYS
3D structure
PDB4q33 Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens Complexed with IMP and A110
ChainF
Resolution2.885 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 F M49 G300 S301 I302 C303 D336 G338 G359 S360 Y383 G385 M386 G387 E411 M48 G175 S176 I177 C178 D211 G213 G234 S235 Y258 G260 M261 G262 E274
BS02 2YA F A248 H249 G387 E411 A123 H124 G262 E274
BS03 2YA F G439 Y440 G302 Y303
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:4q33, PDBe:4q33, PDBj:4q33
PDBsum4q33
PubMed
UniProtA0A0H2YRZ7

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