Structure of PDB 1lrt Chain A

Receptor sequence
>1lrtA (length=338) [Search protein sequence]
AKYYNEPCHTFNEYLLIPGLSTVDCIPSNVNLSTPLVKFQKGQQSEINLK
IPLVSAIMQSVSGEKMAIALAREGGISFIFGSQSIESQAAMVHAVKNFKR
YLVGAGINTRDFRERVPALVEAGADVLCIDSSDGFSEWQKITIGWIRDKY
GDKVKVGAGNIVDGEGFRYLADAGADFIKIGIGGGSICEQKGIGRGQATA
VIDVVAERNKYFEETGIYIPVCSDGGIVYDYHMTLALAMGADFIMLGRYF
ARFEESPTRKVTINGSVMKEYWGEGSSRARNWEEGVDSYVPYAGKLKDNV
EASLNKVKSTMCNCGALTIPQLQSKAKITLVSSVSIVE
3D structure
PDB1lrt Crystal structure of a ternary complex of Tritrichomonas foetus inosine 5'-monophosphate dehydrogenase: NAD+ orients the active site loop for catalysis
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 IMP A M59 G316 S317 C319 D358 G381 R382 Y405 G407 E408 G409 E431 G432 M58 G185 S186 C188 D224 G247 R248 Y271 G273 E274 G275 E284 G285
BS02 TAD A T240 R241 D261 S262 S263 W269 I313 E408 E431 T109 R110 D130 S131 S132 W138 I182 E274 E284 MOAD: Ki=2.3uM
PDBbind-CN: -logKd/Ki=5.64,Ki=2.3uM
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:1lrt, PDBe:1lrt, PDBj:1lrt
PDBsum1lrt
PubMed12403633
UniProtP50097|IMDH_TRIFO Inosine-5'-monophosphate dehydrogenase (Gene Name=IMPDH)

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