Structure of PDB 5n9z Chain C

Receptor sequence
>5n9zC (length=481) Species: 1234817 (Thalassiosira hyalina) [Search protein sequence]
SVSERTRIKSDRYESGVIPYAKMGYWDAAYSVKDTDVLALFRITPQPGVD
PVEAAAAVAGESSTATWTVVWTDLLTACERYRAKAYRVDPVPNSTDVYFA
FIAYECDLFEEASLSNLTASIIGNVFGFKAISALRLEDMRIPHSYLKTFQ
GPATGIIVERERLNKYGTPLLGATVKPKLGLSGKNYGRVVYEGLKGGLDF
LKDDENINSQPFMRWRERFLNCLEGINRAAAATGEVKGSYLNITAATMEE
VYKRAEYAKAIGSVVVMIDLVMGYTAIQSIAYWARENDMLLHLHRAGNST
YARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDVLR
LTELEVNLPFGIFFEMDWASLRRCMPVASGGIHCGQMHQLIHYLGDDVVL
QFGGGTIGHPDGIQAGATANRVALEAMVLARNEGADYFNNQVGPQILRDA
AKTCGPLQTALDLWKDISFNYTSTDTADFAE
3D structure
PDB5n9z Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications.
ChainC
Resolution1.899 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 CAP C T69 N127 T66 N124
BS02 MG C K205 D207 E208 K202 D204 E205
BS03 CAP C T177 K179 K205 D207 E208 H297 R298 H330 K337 L338 S382 G383 G406 G407 T174 K176 K202 D204 E205 H294 R295 H327 K334 L335 S379 G380 G403 G404
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:5n9z, PDBe:5n9z, PDBj:5n9z
PDBsum5n9z
PubMed29925588
UniProtA0A384E0M2

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