Structure of PDB 1upp Chain A

Receptor sequence
>1uppA (length=467) Species: 3562 (Spinacia oleracea) [Search protein sequence]
ASVEFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVA
AESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLF
EEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVE
RDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNS
QPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFAR
ELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHG
MHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDR
SRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLG
HPWGNAPGAVANRVALEACVQARNEGRDLAREGNTIIREATKWSPELAAA
CEVWKEIKFEFPAMDTV
3D structure
PDB1upp Calcium Supports Loop Closure But not Catalysis in Rubisco
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K175 K201 D202 D203 E204 H294 H327 K334
Catalytic site (residue number reindexed from 1) K167 K193 D194 D195 E196 H286 H319 K326
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 CA A K201 D203 E204 K193 D195 E196
BS02 CAP A T173 K175 K201 R295 H327 K334 L335 S379 G380 G403 G404 T165 K167 K193 R287 H319 K326 L327 S371 G372 G395 G396
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:1upp, PDBe:1upp, PDBj:1upp
PDBsum1upp
PubMed14596800
UniProtP00875|RBL_SPIOL Ribulose bisphosphate carboxylase large chain (Gene Name=rbcL)

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