Structure of PDB 5yg8 Chain C

Receptor sequence
>5yg8C (length=322) Species: 70601 (Pyrococcus horikoshii OT3) [Search protein sequence]
AMIVKEVYETAEKIKSMEIRGAGRIARAAAQALMIQAEKSKAKEPEELWN
ELKVASKILYNTRPTAVSLPNALRYVMHRVKAAYLGGADLETLRFTAINS
AKEFIYNSEKAIERIGEIGAKRIEDGDIIMTHCHSKAAISVMKKAFEQGK
NIKVIVTETRPKWQGKITAKELASYGIPVIYIVDSAARHYMKMTDKVVMG
ADSITANGAVINKIGTSLIALTAKEHRVWVMIAAETYKFHPATMLGQLVE
IEMRDPTEVIPEEELRTWPKNIEVWNPAFDVTPPEYIDVIITERGIIPPY
AAIDILKEEFGWALKYKEPWED
3D structure
PDB5yg8 A presumed homologue of the regulatory subunits of eIF2B functions as ribose-1,5-bisphosphate isomerase in Pyrococcus horikoshii OT3.
ChainC
Resolution2.8 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 Q166 A203 D204 N214 K215 K240 M17 R20 G21 A22 R63 C133 S135 K136 A137 Q164 A201 D202 N212 K213 K238
BS03 AMP C R229 W231 D290 R227 W229 D288
BS04 G C L267 P271 I274 L265 P269 I272
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:5yg8, PDBe:5yg8, PDBj:5yg8
PDBsum5yg8
PubMed29382938
UniProtO57947|R15PI_PYRHO Ribose 1,5-bisphosphate isomerase (Gene Name=PH0208)

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