1RCO: Spinach rubisco

Spinach rubisco in complex with the inhibitor D-xylulose-2,2-diol-1,5-bisphosphate. Determined by X-ray diffraction at 2.3 Å resolution. Released 12 Mar 1997.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Spinacia oleracea
Chains
16
Atoms
39,512
Mol. weight
541.61 kDa
Ligands
XDP
Released
12 Mar 1997

Explore 1RCO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1RCO contains 264 α-helices and 224 β-strands across 16 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains B, E, H, K, L, O, R and V: 28 helices, 22 β-strands

ElementResiduesLengthSheet
α-helix21-244
β-strand25110
α-helix29-324
β-strand36-44910
α-helix451
α-helix50-6011
α-helix70-745
α-helix77-804
β-strand83-89710
α-helix901
β-strand97-103710
α-helix105-1073
α-helix113-1208
α-helix124-1263
β-strand12715
β-strand130-1391010
α-helix142-1454
α-helix155-1628
β-strand169-173511
α-helix182-19413
β-strand199-201311
β-strand209112
β-strand212112
α-helix214-23219
β-strand237-241511
α-helix247-26014
β-strand264-268511
α-helix269-2724
α-helix274-28714
β-strand290-294511
α-helix299-3024
β-strand308-309210
α-helix311-32111
β-strand325-327311
β-strand33512
α-helix339-35012
β-strand353-354213
β-strand357114
α-helix358-3603
β-strand362114
β-strand366-367213
α-helix371-3733
β-strand375-379511
α-helix384-3863
α-helix387-3948
β-strand399-401311
α-helix404-4074
α-helix413-43220
α-helix437-44913
α-helix453-46210
Chains C, F, I, M, P, S, T and W: 5 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix2-54
α-helix20-223
α-helix23-3513
α-helix381
β-strand39-45715
β-strand52116
β-strand63116
β-strand68-70315
α-helix80-9314
β-strand98-105815
β-strand110-118915

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ribulose bisphosphate carboxylase/oxygenaseB, E, H, K, L, O, R, Vprotein475Spinacia oleraceaP00875 (AlphaFold model)
Ribulose bisphosphate carboxylase/oxygenaseC, F, I, M, P, S, T, Wprotein123Spinacia oleraceaP00870 (AlphaFold model)
Sequence of entity 1 (B, E, H, K, L, O, R, V), FASTA
>1RCO_1 RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE (chains B, E, H, K, L, O, R, V)
MSPQTETKASVGFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAE
SSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSI
VGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGL
SAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYL
NATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAV
IDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDRSR
GIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVAN
RVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMDTV
Sequence of entity 2 (C, F, I, M, P, S, T, W), FASTA
>1RCO_2 RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE (chains C, F, I, M, P, S, T, W)
MQVWPILNLKKYETLSYLPPLTTDQLARQVDYLLNNKWVPCLEFETDHGFVYREHHNSPG
YYDGRYWTMWKLPMFGCTDPAQVLNELEECKKEYPNAFIRIIGFDSNREVQCISFIAYKP
AGY

Ligands and cofactors

IDNameFormulaCopies
XDPD-xylulose-2,2-diol-1,5-bisphosphateC5 H14 O12 P28

Primary citation

A common structural basis for the inhibition of ribulose 1,5-bisphosphate carboxylase by 4-carboxyarabinitol 1,5-bisphosphate and xylulose 1,5-bisphosphate. Taylor, T.C., Fothergill, M.D., Andersson, I. J Biol Chem (1996) 271:32894-32899. DOI 10.1074/jbc.271.51.32894 · PubMed

Other PDB entries of the same protein (UniProt P00875 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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