Structure of PDB 1rcx Chain H

Receptor sequence
>1rcxH (length=467) Species: 3562 (Spinacia oleracea) [Search protein sequence]
ASVGFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVA
AESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLF
EEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVE
RDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNS
QPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFAR
ELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHG
MHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDR
SRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLG
HPWGNAPGAVANRVALEACVQARNEGRDLAREGNTIIREATKWSPELAAA
CEVWKEIKFEFPAMDTV
3D structure
PDB1rcx The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate.
ChainH
Resolution2.4 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 K334
Catalytic site (residue number reindexed from 1) 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 RUB H T65 W66 N123 T57 W58 N115
BS02 RUB H K175 E204 H294 R295 H327 K334 S379 G380 G403 G404 K167 E196 H286 R287 H319 K326 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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Biological Process
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Cellular Component
External links
PDB RCSB:1rcx, PDBe:1rcx, PDBj:1rcx
PDBsum1rcx
PubMed9034362
UniProtP00875|RBL_SPIOL Ribulose bisphosphate carboxylase large chain (Gene Name=rbcL)

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