Structure of PDB 5yfu Chain C

Receptor sequence
>5yfuC (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.
ChainC
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 AMP C N209 A211 L250 V251 V283 N207 A209 L248 V249 V281
BS02 RUB C M19 R22 G23 A24 R65 C135 S137 K138 A139 A203 D204 N214 K215 K240 M17 R20 G21 A22 R63 C133 S135 K136 A137 A201 D202 N212 K213 K238
BS03 AMP C R229 W231 D290 R227 W229 D288
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
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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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