Structure of PDB 4xtd Chain A

Receptor sequence
>4xtdA (length=377) Species: 284811 (Eremothecium gossypii ATCC 10895) [Search protein sequence]
TYRDAATALEHLATYAEKDGLSVEQLMGGLTYNDFLVLPGKIDFPSSEVV
LSSRLTKKITLNAPFVSSPMDTVTEADMAIHMALLGGIGIIHHNCTAEEQ
AEMVRRVKKYENPLASKSADTKQLLCGAAIGTIDADRQRLAMLVEAGLDV
VVLDSSQGNSVFQINMIKWIKETFPDLQVIAGNVVTREQAASLIHAGADG
LRIGMGSGSICITQEVMACGRPQGTAVYNVTQFANQFGVPCIADGGVQNI
GHITKAIALGASTVMMGGMLAGTTESPGEYFFRGKRLKTYRGMGSIDAMQ
KLVAQGVTGSVIDKGSIKKYIPYLYNGLQHSCQDIGVRSLVEFREKVDSG
SVRFEFRTPSAQLEGGVHNLHSYERLF
3D structure
PDB4xtd Increased riboflavin production by manipulation of inosine 5'-monophosphate dehydrogenase in Ashbya gossypii.
ChainA
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 A S74 M76 R325 G331 S332 I333 C334 D367 G390 G391 Y414 G416 M417 G418 S68 M70 R202 G208 S209 I210 C211 D244 G267 G268 Y290 G292 M293 G294
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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