Structure of PDB 5oya Chain B

Receptor sequence
>5oyaB (length=469) Species: 163503 (Chaetoceros socialis) [Search protein sequence]
RYESGVIPYAKMGYWDAAYTVKDTDVLALFRITPQPGVDPVEAAAAVAGE
SSTATWTVVWTDLLTACERYRAKAYRVDPVPNSTDVYFAFIAYECDLFEE
ASLANLTASIIGNVFGFKAISALRLEDMRIPHSYLKTFQGPATGIIVERE
RLNKYGTPLLGATVKPKLGLSGKNYGRVVYEGLKGGLDFLKDDENINSQP
FMRWRERFLNCLEGINRASAATGEVKGSYLNVTAATMEEVYKRAEYAKAI
GSIVVMIDLVMGYTAIQSIAYWARENDMLLHLHRAGNSTYARQKNHGINF
RVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDILRLTELEVNLPFG
IFFEMDWASLRRCMPVASGGIHCGQMHQLIHYLGDDVVLQFGGGTIGHPD
GIQAGATANRVALEAMVLARNEGADYFNNQVGPQILRDAAKTCGPLQTAL
DLWKDISFNYTSTDTADFS
3D structure
PDB5oya Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications.
ChainB
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.39: ribulose-bisphosphate carboxylase.
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 MG B K205 D207 E208 K191 D193 E194
BS02 CAP B T177 K179 K205 D207 E208 H297 R298 H330 K337 L338 S382 G383 G406 G407 T163 K165 K191 D193 E194 H283 R284 H316 K323 L324 S368 G369 G392 G393
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004497 monooxygenase activity
GO:0016829 lyase activity
GO:0016984 ribulose-bisphosphate carboxylase activity
GO:0046872 metal ion binding
Biological Process
GO:0015977 carbon fixation
GO:0019253 reductive pentose-phosphate cycle
Cellular Component
GO:0009536 plastid

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5oya, PDBe:5oya, PDBj:5oya
PDBsum5oya
PubMed29925588
UniProtA0A3B6UEF4

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