Structure of PDB 6rpu Chain A

Receptor sequence
>6rpuA (length=432) Species: 284811 (Eremothecium gossypii ATCC 10895) [Search protein sequence]
YRDAATALEHLATYAEKDGLSVEQLMDSKTRGGLTYNDFLVLPGKIDFPS
SEVVLSSRLTKKITLNAPFVSSPMDTVTEADMAIHMALLGGIGIIHHNCT
AEEQAEMVRRVKKYENGFINAPVVVGPDATVADVRRMKNEFGFAGFPVTD
DGKPTGKLQGIITSRDIQFVEDETLLVSEIMTKDVITGKQGINLEEANQI
LKNTKKGKLPIVDGCLVSMLSRTDLMKNQSYPLASKSADTKQLLCGAAIG
TIDADRQRLAMLVEAGLDVVVLDSSQGNSVFQINMIKWIKETFPDLQVIA
GNVVTREQAASLIHAADGLRIGMMACGRPQGTAVYNVTQFANQFGVPCIA
DGGVQNIGHITKAIALGASTVMMGGMLAGTTESPGDKGSIKKYIPYLYNG
LQHSCQDIGVRSLVEFREKVDSGSVRFEFRTP
3D structure
PDB6rpu The Bateman domain of IMP dehydrogenase is a binding target for dinucleoside polyphosphates.
ChainA
Resolution2.11 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 G5P A V125 F145 A146 G147 T165 S166 D168 T184 V187 I188 G209 K210 T227 D228 K231 V123 F143 A144 G145 T163 S164 D166 T182 V185 I186 G207 K208 T223 D224 K227
BS02 GDP A E117 N118 G119 N200 L229 N232 K240 K245 E115 N116 G117 N198 L225 N228 K236 K241
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0003938 IMP dehydrogenase activity
GO:0005524 ATP binding
GO:0016491 oxidoreductase activity
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6rpu, PDBe:6rpu, PDBj:6rpu
PDBsum6rpu
PubMed31416831
UniProtQ756Z6

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