Structure of PDB 4z0g Chain B

Receptor sequence
>4z0gB (length=390) Species: 284811 (Eremothecium gossypii ATCC 10895) [Search protein sequence]
MTYRDAATALEHLATYAEKDGLSVEQLMDTRGGLTYNDFLVLPGKIDFPS
SEVVLSSRLTKKITLNAPFVSSPMDTVTEADMAIHMALLGGIGIIHHNCT
AEEQAEMVRRVKKYENDGPLASKSADTKQLLCGAAIGTIDADRQRLAMLV
EAGLDVVVLDSSQGNSVFQINMIKWIKETFPDLQVIAGNVVTREQAASLI
HAGADGLRIGMGSGSICITQEVMACGRPQGTAVYNVTQFANQFGVPCIAD
GGVQNIGHITKAIALGASTVMMGGMLAGTTESPGEYFFRGKRLKTYRGMG
SIDAMQKTDVKVLVAQGVTGSVIDKGSIKKYIPYLYNGLQHSCQDIGVRS
LVEFREKVDSGSVRFEFRTPSAQLEGGVHNLHSYEKRLFD
3D structure
PDB4z0g Guanine nucleotide binding to the Bateman domain mediates the allosteric inhibition of eukaryotic IMP dehydrogenases.
ChainB
Resolution1.25 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 5GP B S74 M76 R325 G331 S332 I333 C334 T336 D367 G390 G391 Y414 G416 M417 G418 Q448 S72 M74 R208 G214 S215 I216 C217 T219 D250 G273 G274 Y296 G298 M299 G300 Q316 MOAD: Ki=600uM
BS02 5GP B S283 V284 F285 S166 V167 F168 MOAD: Ki=600uM
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

View graph for
Molecular Function

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Biological Process
External links
PDB RCSB:4z0g, PDBe:4z0g, PDBj:4z0g
PDBsum4z0g
PubMed26558346
UniProtQ756Z6

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