Structure of PDB 1me8 Chain A

Receptor sequence

>1me8A (length=357)

AKYYNEPCHTFNEYLLIPGLSTVDCIPSNVNLSTPLVKFQKGQQSEINLK
IPLVSAIMQSVSGEKMAIALAREGGISFIFGSQSIESQAAMVHAVKNFKA
HNELVDSQKRYLVGAGINTRDFRERVPALVEAGADVLCIDSSDGFSEWQK
ITIGWIREKYGDKVKVGAGNIVDGEGFRYLADAGADFIKIGIGGGSICIT
REQKGIGRGQATAVIDVVAERNKYFEETGIYIPVCSDGGIVYDYHMTLAL
AMGADFIMLGRYFARFEESPTRKVTINGSVMKEYWGEGSSRARNWEGVDS
YVPYAGKLKDNVEASLNKVKSTMCNCGALTIPQLQSKAKITLVSSVSIVE
GGAHDVI

3D structure

• PDB: 1me8 Crystal Structure of Tritrichomonas foetus Inosine Monophosphate Dehydrogenase in Complex with the Inhibitor Ribavirin Monophosphate Reveals a Catalysis-dependent Ion-binding Site
• Chain: A
• Resolution: 1.9 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	RVP	A	M59 G316 S317 I318 C319 D358 L380 G381 R382 Y405 G407 E408 G409	M58 G195 S196 I197 C198 D237 L259 G260 R261 Y284 G286 E287 G288	MOAD: Ki=65nM PDBbind-CN: -logKd/Ki=7.19,Ki=65nM

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0003824 catalytic activity
• GO:0003938 IMP dehydrogenase activity
• GO:0016491 oxidoreductase activity
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006164 purine nucleotide biosynthetic process
• GO:0006177 GMP biosynthetic process
• GO:0006183 GTP biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0032991 protein-containing complex

External links

• PDB: RCSB:1me8, PDBe:1me8, PDBj:1me8
• PDBsum: 1me8
• PubMed: 12235158
• UniProt: P50097|IMDH_TRIFO Inosine-5'-monophosphate dehydrogenase (Gene Name=IMPDH)