Structure of PDB 1mei Chain A

Receptor sequence
>1meiA (length=351) [Search protein sequence]
AKYYNEPCHTFNEYLLIPGLSTVDCIPSNVNLSTPLVKFQKGQQSEINLK
IPLVSAIMQSVSGEKMAIALAREGGISFIFGSQSIESQAAMVHAVKNFKA
HNELVDSQKRYLVGAGINTRDFRERVPALVEAGADVLCIDSSDGFSEWQK
ITIGWIREKYGDKVKVGAGNIVDGEGFRYLADAGADFIKIGIGGGSICIT
REQKGIGRGQATAVIDVVAERNKYFEETGIYIPVCSDGGIVYDYHMTLAL
AMGADFIMLGRYFARFEESPTRKVTINGSVMKEYWGEGSSRARNWSFEEG
VDSYVPYAGKLKDNVEASLNKVKSTMCNCGALTIPQLQSKAKITLVSSVS
I
3D structure
PDB1mei 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
ChainA
Resolution2.2 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 K A P19 G20 L21 S22 N460 P18 G19 L20 S21 N328
BS02 XMP A G316 S317 I318 C319 D358 G381 R382 Y405 G407 E408 G409 G432 G195 S196 I197 C198 D237 G260 R261 Y284 G286 E287 G288 G300
BS03 MOA A D261 S262 S263 G312 E408 G409 D140 S141 S142 G191 E287 G288
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1mei, PDBe:1mei, PDBj:1mei
PDBsum1mei
PubMed12559919
UniProtP50097|IMDH_TRIFO Inosine-5'-monophosphate dehydrogenase (Gene Name=IMPDH)

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