Structure of PDB 5n9z Chain H Binding Site BS01

Receptor Information
>5n9z Chain H (length=481) Species: 1234817 (Thalassiosira hyalina) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SVSERTRIKSDRYESGVIPYAKMGYWDAAYSVKDTDVLALFRITPQPGVD
PVEAAAAVAGESSTATWTVVWTDLLTACERYRAKAYRVDPVPNSTDVYFA
FIAYECDLFEEASLSNLTASIIGNVFGFKAISALRLEDMRIPHSYLKTFQ
GPATGIIVERERLNKYGTPLLGATVKPKLGLSGKNYGRVVYEGLKGGLDF
LKDDENINSQPFMRWRERFLNCLEGINRAAAATGEVKGSYLNITAATMEE
VYKRAEYAKAIGSVVVMIDLVMGYTAIQSIAYWARENDMLLHLHRAGNST
YARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDVLR
LTELEVNLPFGIFFEMDWASLRRCMPVASGGIHCGQMHQLIHYLGDDVVL
QFGGGTIGHPDGIQAGATANRVALEAMVLARNEGADYFNNQVGPQILRDA
AKTCGPLQTALDLWKDISFNYTSTDTADFAE
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain5n9z Chain H Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5n9z Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications.
Resolution1.899 Å
Binding residue
(original residue number in PDB)
K205 D207 E208
Binding residue
(residue number reindexed from 1)
K202 D204 E205
Annotation score1
Enzymatic activity
Enzyme Commision number 4.1.1.39: ribulose-bisphosphate carboxylase.
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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