Structure of PDB 6ftl Chain A

Receptor sequence
>6ftlA (length=482) Species: 267567 (Skeletonema marinoi) [Search protein sequence]
QSVSERTRIKSDRYESGVIPYAKMGYWDASYTVKDTDVLALFRITPQPGV
DPVEAAAAVAGESSTATWTVVWTDLLTACERYRAKAYRVDPVPNSADVFF
AFIAYECDLFEEASLANLTASIIGNVFGFKAVSALRLEDMRIPHSYLKTF
QGPATGIIVERERLNKYGTPLLGATVKPKLGLSGKNYGRVVYEGLKGGLD
FLKDDENINSQPFMRWRERFLNCMEGINRASAATGEVKGSYLNITAATME
EVYKRAEYAKAVGSIVVMIDLVMGYTAIQSIAYWARENDMLLHLHRAGNS
TYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDIL
RLTELEVNLPFGIFFEMDWASLRRCMPVASGGIHCGQMHQLIHYLGDDVV
LQFGGGTIGHPDGIQAGATANRVALESMVLARNEGVDYFDQQVGPQILRD
AAKTCGPLQTALDLWKDISFDYTSTDTADFAE
3D structure
PDB6ftl Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications.
ChainA
Resolution2.6 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 A K205 D207 E208 K203 D205 E206
BS02 CAP A T177 K179 K181 K205 E208 H297 R298 H330 K337 L338 S382 G383 G406 G407 T175 K177 K179 K203 E206 H295 R296 H328 K335 L336 S380 G381 G404 G405
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:6ftl, PDBe:6ftl, PDBj:6ftl
PDBsum6ftl
PubMed29925588
UniProtA0A3B6UEX0

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