Structure of PDB 1bxn Chain C

Receptor sequence
>1bxnC (length=445) Species: 106590 (Cupriavidus necator) [Search protein sequence]
YKMGYWDGDYVPKDTDLLALFRITPQDGVDPVEAAAAVAGESSTATWTVV
WTDRLTACDMYRAKAYRVDPVPNNPEQFFCYVAYDLSLFEEGSIANLTAS
IIGNVFSFKPIKAARLEDMRFPVAYVKTFAGPSTGIIVERERLDKFGRPL
LGATTKPKLGLSGRNYGRVVYEGLKGGLDFMKDDENINSQPFMHWRDRFL
FVMDAVNKASAATGEVKGSYLNVTAGTMEEMYRRAEFAKSLGSVIIMVDL
IVGWTCIQSMSNWCRQNDMILHLHRAGHGTYTRQKNHGVSFRVIAKWLRL
AGVDHMHTGTAVGKLEGDPLTVQGYYNVCRDAYTQTDLTRGLFFDQDWAS
LRKVMPVASGGIHAGQMHQLIHLFGDDVVLQFGGGTIGHPQGIQAGATAN
RVALEAMVLARNEGRDILNEGPEILRDAARWCGPLRAALDTWGDI
3D structure
PDB1bxn The crystal structure of rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded beta-barrel formed by beta-strands from four subunits.
ChainC
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K178 K204 D205 D206 E207 H296 H329 K336
Catalytic site (residue number reindexed from 1) K156 K182 D183 D184 E185 H274 H307 K314
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 PO4 C R297 H329 S381 R275 H307 S359
BS02 PO4 C G382 G405 G406 G360 G383 G384
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1bxn, PDBe:1bxn, PDBj:1bxn
PDBsum1bxn
PubMed10329167
UniProtP0C2C2|RBL1C_CUPNE Ribulose bisphosphate carboxylase large chain, chromosomal (Gene Name=cbbL1)

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