Structure of PDB 5yfu Chain A

Receptor sequence
>5yfuA (length=322) Species: 70601 (Pyrococcus horikoshii OT3) [Search protein sequence]
AMIVKEVYETAEKIKSMEIRGAGRIARAAAQALMIQAEKSKAKEPEELWN
ELKVASKILYNTRPTAVSLPNALRYVMHRVKAAYLGGADLETLRFTAINS
AKEFIYNSEKAIERIGEIGAKRIEDGDIIMTHCHSKAAISVMKKAFEQGK
NIKVIVTETRPKWQGKITAKELASYGIPVIYIVDSAARHYMKMTDKVVMG
ADSITANGAVINKIGTSLIALTAKEHRVWVMIAAETYKFHPATMLGQLVE
IEMRDPTEVIPEEELRTWPKNIEVWNPAFDVTPPEYIDVIITERGIIPPY
AAIDILKEEFGWALKYKEPWED
3D structure
PDB5yfu A presumed homologue of the regulatory subunits of eIF2B functions as ribose-1,5-bisphosphate isomerase in Pyrococcus horikoshii OT3.
ChainA
Resolution2.35 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 5.3.1.29: ribose-1,5-bisphosphate isomerase.
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 RUB A M19 R22 G23 A24 G25 R65 C135 S137 K138 A139 D204 N214 K215 K240 M17 R20 G21 A22 G23 R63 C133 S135 K136 A137 D202 N212 K213 K238
BS02 AMP A R229 W231 D290 R227 W229 D288
BS03 AMP A N209 A211 L250 V251 V283 N207 A209 L248 V249 V281
Gene Ontology
Molecular Function
GO:0016853 isomerase activity
GO:0043917 ribose 1,5-bisphosphate isomerase activity
GO:0046523 S-methyl-5-thioribose-1-phosphate isomerase activity
Biological Process
GO:0019323 pentose catabolic process
GO:0019509 L-methionine salvage from methylthioadenosine
GO:0044237 cellular metabolic process
GO:0044249 cellular biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5yfu, PDBe:5yfu, PDBj:5yfu
PDBsum5yfu
PubMed29382938
UniProtO57947|R15PI_PYRHO Ribose 1,5-bisphosphate isomerase (Gene Name=PH0208)

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