Structure of PDB 4xtd Chain B

Receptor sequence
>4xtdB (length=383) Species: 284811 (Eremothecium gossypii ATCC 10895) [Search protein sequence]
TYRDAATALEHLATYAEKDGLSVEQLMDKTRGGLTYNDFLVLPGKIDFPS
SEVVLSSRLTKKITLNAPFVSSPMDTVTEADMAIHMALLGGIGIIHHNCT
AEEQAEMVRRVKKYENPLASKSADTKQLLCGAAIGTIDADRQRLAMLVEA
GLDVVVLDSSQGNSVFQINMIKWIKETFPDLQVIAGNVVTREQAASLIHA
GADGLRIGMGSGSICITQEVMACGRPQGTAVYNVTQFANQFGVPCIADGG
VQNIGHITKAIALGASTVMMGGMLAGTTESPGEYFFRDGKRLKTYRGMGS
IDAMQKVLVAQGVTGSVIDKGSIKKYIPYLYNGLQHSCQDIGVRSLVEFR
EKVDSGSVRFEFRTPSAQLEGGVHNLHSYERLF
3D structure
PDB4xtd Increased riboflavin production by manipulation of inosine 5'-monophosphate dehydrogenase in Ashbya gossypii.
ChainB
Resolution2.05 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 B S74 M76 R325 G331 S332 I333 C334 D367 G390 G391 Y414 G416 M417 G418 S72 M74 R206 G212 S213 I214 C215 D248 G271 G272 Y295 G297 M298 G299
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

View graph for
Biological Process
External links
PDB RCSB:4xtd, PDBe:4xtd, PDBj:4xtd
PDBsum4xtd
PubMed26150243
UniProtQ756Z6

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