Structure of PDB 4z87 Chain B

Receptor sequence
>4z87B (length=498) Species: 284811 (Eremothecium gossypii ATCC 10895) [Search protein sequence]
TYRDAATALEHLATYAEKDGLSVEQLMDSKTRGGLTYNDFLVLPGKIDFP
SSEVVLSSRLTKKITLNAPFVSSPMDTVTEADMAIHMALLGGIGIIHHNC
TAEEQAEMVRRVKKYENGFINAPVVVGPDATVADVRRMKNEFGFAGFPVT
DDGKPTGKLQGIITSRDIQFVEDETLLVSEIMTKDVITGKQGINLEEANQ
ILKNTKKGKLPIVDEAGCLVSMLSRTDLMKNQSYPLASKSADTKQLLCGA
AIGTIDADRQRLAMLVEAGLDVVVLDSSQGNSVFQINMIKWIKETFPDLQ
VIAGNVVTREQAASLIHAGADGLRIGMGSGSICITQEVMACGRPQGTAVY
NVTQFANQFGVPCIADGGVQNIGHITKAIALGASTVMMGGMLAGTTESPG
EYFFRDGKRLKTYRGMGSIDAMQVAQGVTGSVIDKGSIKKYIPYLYNGLQ
HSCQDIGVRSLVEFREKVDSGSVRFEFRTPSAQLEGGVHNLHSYELFD
3D structure
PDB4z87 Guanine nucleotide binding to the Bateman domain mediates the allosteric inhibition of eukaryotic IMP dehydrogenases.
ChainB
Resolution2.25 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 1.1.1.205: IMP dehydrogenase.
Interaction with ligand
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4z87, PDBe:4z87, PDBj:4z87
PDBsum4z87
PubMed26558346
UniProtQ756Z6

[Back to BioLiP]