1AUS: Activated unliganded spinach rubisco

Activated unliganded spinach rubisco. Determined by X-ray diffraction at 2.2 Å resolution. Released 15 Oct 1995.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Spinacia oleracea
Chains
8
Atoms
18,149
Mol. weight
269.77 kDa
Ligands
MG
Released
15 Oct 1995

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

Secondary structure: helices and β-sheets

1AUS contains 132 α-helices and 104 β-strands across 8 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 L, M, N and O: 28 helices, 20 β-strands

ElementResiduesLengthSheet
α-helix21-244
β-strand2511
α-helix29-324
β-strand36-4491
α-helix451
α-helix50-6011
α-helix70-745
α-helix77-793
β-strand83-8971
α-helix901
β-strand97-10371
α-helix105-1073
α-helix113-1219
α-helix124-1263
β-strand130-139101
α-helix142-1454
α-helix155-1628
β-strand169-17352
α-helix182-19413
β-strand199-20132
β-strand20913
β-strand21213
α-helix214-23219
β-strand237-24152
α-helix247-26014
β-strand264-26852
α-helix269-2724
α-helix274-28714
β-strand290-29452
α-helix298-3025
β-strand308-30921
α-helix311-32111
β-strand325-32732
α-helix339-35012
β-strand353-35424
β-strand35715
α-helix358-3603
β-strand36215
β-strand366-36724
α-helix371-3733
β-strand375-37842
α-helix384-3863
α-helix387-3948
β-strand399-40132
α-helix404-4074
α-helix413-43220
α-helix437-44913
α-helix453-4619
Chains S, T, U and V: 5 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix3-53
α-helix19-224
α-helix23-3614
α-helix381
β-strand39-4576
β-strand5217
β-strand6317
β-strand68-7036
α-helix80-9314
β-strand98-10586
β-strand110-11896

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ribulose bisphosphate carboxylase/oxygenaseL, M, N, Oprotein475Spinacia oleraceaP00875 (AlphaFold model)
Ribulose bisphosphate carboxylase/oxygenaseS, T, U, Vprotein123Spinacia oleraceaQ43832 (AlphaFold model)
Sequence of entity 1 (L, M, N, O), FASTA
>1AUS_1 RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE (chains L, M, N, O)
MSPQTETKASVGFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAE
SSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSI
VGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGL
SAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYL
NATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAV
IDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDRSR
GIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVAN
RVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMDTV
Sequence of entity 2 (S, T, U, V), FASTA
>1AUS_2 RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE (chains S, T, U, V)
MQVWPILNLKKYETLSYLPPLTTDQLARQVDYLLNNKWVPCLEFETDHGFVYREHHNSPG
YYDGRYWTMWKLPMFGCTDPAQVLNELEECKKEYPNAFIRIIGFDSNREVQCISFIAYKP
AGY

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg4

Water and common crystallization additives (FMT) are not listed.

Primary citation

Structure of a product complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase. Taylor, T.C., Andersson, I. Biochemistry (1997) 36:4041-4046. DOI 10.1021/bi962818w · PubMed

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

Browse structure collections

About this viewer

MolViewer shows 1AUS directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.