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.
Explore 1RCO in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 21-24 | 4 | |
| β-strand | 25 | 1 | 10 |
| α-helix | 29-32 | 4 | |
| β-strand | 36-44 | 9 | 10 |
| α-helix | 45 | 1 | |
| α-helix | 50-60 | 11 | |
| α-helix | 70-74 | 5 | |
| α-helix | 77-80 | 4 | |
| β-strand | 83-89 | 7 | 10 |
| α-helix | 90 | 1 | |
| β-strand | 97-103 | 7 | 10 |
| α-helix | 105-107 | 3 | |
| α-helix | 113-120 | 8 | |
| α-helix | 124-126 | 3 | |
| β-strand | 127 | 1 | 5 |
| β-strand | 130-139 | 10 | 10 |
| α-helix | 142-145 | 4 | |
| α-helix | 155-162 | 8 | |
| β-strand | 169-173 | 5 | 11 |
| α-helix | 182-194 | 13 | |
| β-strand | 199-201 | 3 | 11 |
| β-strand | 209 | 1 | 12 |
| β-strand | 212 | 1 | 12 |
| α-helix | 214-232 | 19 | |
| β-strand | 237-241 | 5 | 11 |
| α-helix | 247-260 | 14 | |
| β-strand | 264-268 | 5 | 11 |
| α-helix | 269-272 | 4 | |
| α-helix | 274-287 | 14 | |
| β-strand | 290-294 | 5 | 11 |
| α-helix | 299-302 | 4 | |
| β-strand | 308-309 | 2 | 10 |
| α-helix | 311-321 | 11 | |
| β-strand | 325-327 | 3 | 11 |
| β-strand | 335 | 1 | 2 |
| α-helix | 339-350 | 12 | |
| β-strand | 353-354 | 2 | 13 |
| β-strand | 357 | 1 | 14 |
| α-helix | 358-360 | 3 | |
| β-strand | 362 | 1 | 14 |
| β-strand | 366-367 | 2 | 13 |
| α-helix | 371-373 | 3 | |
| β-strand | 375-379 | 5 | 11 |
| α-helix | 384-386 | 3 | |
| α-helix | 387-394 | 8 | |
| β-strand | 399-401 | 3 | 11 |
| α-helix | 404-407 | 4 | |
| α-helix | 413-432 | 20 | |
| α-helix | 437-449 | 13 | |
| α-helix | 453-462 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-5 | 4 | |
| α-helix | 20-22 | 3 | |
| α-helix | 23-35 | 13 | |
| α-helix | 38 | 1 | |
| β-strand | 39-45 | 7 | 15 |
| β-strand | 52 | 1 | 16 |
| β-strand | 63 | 1 | 16 |
| β-strand | 68-70 | 3 | 15 |
| α-helix | 80-93 | 14 | |
| β-strand | 98-105 | 8 | 15 |
| β-strand | 110-118 | 9 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ribulose bisphosphate carboxylase/oxygenase | B, E, H, K, L, O, R, V | protein | 475 | Spinacia oleracea | P00875 (AlphaFold model) |
| Ribulose bisphosphate carboxylase/oxygenase | C, F, I, M, P, S, T, W | protein | 123 | Spinacia oleracea | P00870 (AlphaFold model) |
>1RCO_1 RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE (chains B, E, H, K, L, O, R, V) MSPQTETKASVGFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAE SSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSI VGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGL SAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYL NATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAV IDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDRSR GIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVAN RVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMDTV
>1RCO_2 RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE (chains C, F, I, M, P, S, T, W) MQVWPILNLKKYETLSYLPPLTTDQLARQVDYLLNNKWVPCLEFETDHGFVYREHHNSPG YYDGRYWTMWKLPMFGCTDPAQVLNELEECKKEYPNAFIRIIGFDSNREVQCISFIAYKP AGY
| ID | Name | Formula | Copies |
|---|---|---|---|
| XDP | D-xylulose-2,2-diol-1,5-bisphosphate | C5 H14 O12 P2 | 8 |
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:
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