Structure of PDB 1mew Chain A

Receptor sequence

>1mewA (length=344)

AKYYNEPCHTFNEYLLIPGLSTVDCIPSNVNLSTPLVKFQKGQQSEINLK
IPLVSAIMQSVSGEKMAIALAREGGISFIFGSQSIESQAAMVHAVKNFKA
HNELVDSQKRYLVGAGINTRDFRERVPALVEAGADVLCIDSSDGFSEWQK
ITIGWIREKYGDKVKVGAGNIVDGEGFRYLADAGADFIKIGIGGGSREQK
GIGRGQATAVIDVVAERNKYFEETGIYIPVCSDGGIVYDYHMTLALAMGA
DFIMLGRYFARFEESPTRKVTINGSVMKEYWGEGSSRARNWEGVDSYVPY
AGKLKDNVEASLNKVKSTMCNCGALTIPQLQSKAKITLVSSVSI

3D structure

• PDB: 1mew Crystal Structures of Tritrichomonas foetus Inosine Monophosphate Dehydrogenase in Complex with Substrate, Cofactor and Analogs: A Structural Basis for the Random-in Ordered-out Kinetic Mechanism
• Chain: A
• Resolution: 2.15 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	K	A	D264 F266	D143 F145
BS02	XMP	A	G316 S317 D358 L380 G381 R382 Y405 G407 E408 G409 E431 G432	G195 S196 D233 L255 G256 R257 Y280 G282 E283 G284 E292 G293
BS03	NAD	A	T240 R241 D261 S262 S263 W269 E408 E431	T119 R120 D140 S141 S142 W148 E283 E292

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:1mew, PDBe:1mew, PDBj:1mew
• PDBsum: 1mew
• PubMed: 12559919
• UniProt: P50097|IMDH_TRIFO Inosine-5'-monophosphate dehydrogenase (Gene Name=IMPDH)