Structure of PDB 5n9z Chain H

Receptor sequence
>5n9zH (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.
ChainH
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 MG H K205 D207 E208 K202 D204 E205
BS02 CAP H 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
BS03 CAP H T69 N127 T66 N124
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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