Structure of PDB 5yg7 Chain A

Receptor sequence
>5yg7A (length=322) Species: 70601 (Pyrococcus horikoshii OT3) [Search protein sequence]
AMIVKEVYETAEKIKSMEIRGAGRIARAAAQALMIQAEKSKAKEPEELWN
ELKVASKILYNTRPTAVSLPNALRYVMHRVKAAYLGGADLETLRFTAINS
AKEFIYNSEKAIERIGEIGAKRIEDGDIIMTHCHSKAAISVMKKAFEQGK
NIKVIVTETRPKWQGKITAKELASYGIPVIYIVDSAARHYMKMTDKVVMG
ANSITANGAVINKIGTSLIALTAKEHRVWVMIAAETYKFHPATMLGQLVE
IEMRDPTEVIPEEELRTWPKNIEVWNPAFDVTPPEYIDVIITERGIIPPY
AAIDILKEEFGWALKYKEPWED
3D structure
PDB5yg7 A presumed homologue of the regulatory subunits of eIF2B functions as ribose-1,5-bisphosphate isomerase in Pyrococcus horikoshii OT3.
ChainA
Resolution2.5 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 RI2 A M19 R22 G23 A24 G25 R65 S137 K138 A139 A203 N204 N214 K215 K240 F281 M17 R20 G21 A22 G23 R63 S135 K136 A137 A201 N202 N212 K213 K238 F279 MOAD: Kd=10uM
BS02 G A T207 N209 L250 V251 V283 T205 N207 L248 V249 V281
BS03 G A R124 R229 W231 D290 R122 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:5yg7, PDBe:5yg7, PDBj:5yg7
PDBsum5yg7
PubMed29382938
UniProtO57947|R15PI_PYRHO Ribose 1,5-bisphosphate isomerase (Gene Name=PH0208)

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