Structure of PDB 1aus Chain N

Receptor sequence
>1ausN (length=439) Species: 3562 (Spinacia oleracea) [Search protein sequence]
YKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTV
WTDGLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTS
IVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPL
LGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFL
FCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFARELGVPIVMHDY
LTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALR
LSGGDHIHSGTVVERDITLGFVDLLRDDYTEKDRSRGIYFTQSWVSTPGV
LPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVAL
EACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWK
3D structure
PDB1aus Structure of a product complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase.
ChainN
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D203 E204 H294 H327
Catalytic site (residue number reindexed from 1) D184 E185 H275 H308
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 N D203 E204 D184 E185
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:0009853 photorespiration
GO:0015977 carbon fixation
GO:0015979 photosynthesis
GO:0019253 reductive pentose-phosphate cycle
Cellular Component
GO:0009507 chloroplast

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Cellular Component
External links
PDB RCSB:1aus, PDBe:1aus, PDBj:1aus
PDBsum1aus
PubMed9092835
UniProtP00875|RBL_SPIOL Ribulose bisphosphate carboxylase large chain (Gene Name=rbcL)

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