Structure of PDB 4xti Chain A

Receptor sequence
>4xtiA (length=373) Species: 284811 (Eremothecium gossypii ATCC 10895) [Search protein sequence]
YRDAATALEHLATYAEKDGLSVEQLMGGLTYNDFLVLPGKIDFPSSEVVL
SSRLTKKITLNAPFVSSPMDTVTEADMAIHMALLGGIGIIHHNCTAEEQA
EMVRRVKKYLASKSADTKQLLCGAAIGTIDADRQRLAMLVEAGLDVVVLD
SSQGNSVFQINMIKWIKETFPDLQVIAGNVVTREQAASLIHAGADGLRIG
MGSGSICITQEVMACGRPQGTAVYNVTQFANQFGVPCIADGGVQNIGHIT
KAIALGASTVMMGGMLAGTTESPGEYFFRKRLKTYRGMGSIDAMQKLVAQ
GVTGSVIDKGSIKKYIPYLYNGLQHSCQDIGVRSLVEFREKVDSGSVRFE
FRTPSAQLEGGVHNLHSYEKRLF
3D structure
PDB4xti Increased riboflavin production by manipulation of inosine 5'-monophosphate dehydrogenase in Ashbya gossypii.
ChainA
Resolution1.5 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 G369 G390 Y414 G416 M417 G418 S67 M69 R198 G204 S205 I206 C207 D240 G242 G263 Y285 G287 M288 G289
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

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Molecular Function
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Biological Process
External links
PDB RCSB:4xti, PDBe:4xti, PDBj:4xti
PDBsum4xti
PubMed26150243
UniProtQ756Z6

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