Structure of PDB 3axm Chain H

Receptor sequence
>3axmH (length=444) Species: 39947 (Oryza sativa Japonica Group) [Search protein sequence]
GFKAGVKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTG
TWTTVWTDGLTSLDRYKGRCYHIEPVVGEDNQYIAYVAYPLDLFEEGSVT
NMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNK
YGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRW
RDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPI
VMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVL
AKALRMSGGDHIHAGTVVEREMTLGFVDLLRDDFIEKDRARGIFFTQDWV
SMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAA
NRVALEACVQARNEGRDLAREGNEIIRSACKWSPELAAACEIWK
3D structure
PDB3axm Crystal structure of rice Rubisco and implications for activation induced by positive effectors NADPH and 6-phosphogluconate
ChainH
Resolution1.65 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) D189 E190 H280 H313
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 K201 D203 E204 K187 D189 E190
BS02 6PG H K175 K201 R295 H298 S379 K161 K187 R281 H284 S360 MOAD: Ki=8.5uM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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
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:3axm, PDBe:3axm, PDBj:3axm
PDBsum3axm
PubMed22609438
UniProtP0C512|RBL_ORYSJ Ribulose bisphosphate carboxylase large chain (Gene Name=rbcL)

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