1AA1: Activated spinach rubisco

Activated spinach rubisco in complex with the product 3-phosphoglycerate. Determined by X-ray diffraction at 2.2 Å resolution. Released 7 Jul 1997.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Spinacia oleracea
Chains
8
Atoms
18,956
Mol. weight
271.25 kDa
Ligands
3PG, MG
Released
7 Jul 1997

Explore 1AA1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1AA1 contains 124 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 B, E, H and L: 27 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand2518
α-helix29-324
β-strand36-4498
α-helix451
α-helix50-6011
α-helix70-745
α-helix77-793
β-strand83-8978
α-helix901
β-strand97-10378
α-helix105-1073
α-helix113-1219
α-helix124-1263
β-strand130-139108
α-helix142-1454
α-helix155-1628
β-strand169-17359
α-helix182-19413
β-strand199-20139
β-strand209110
β-strand212110
α-helix214-23219
β-strand237-24159
α-helix247-26014
β-strand264-26859
α-helix269-2724
α-helix274-28714
β-strand290-29459
α-helix298-3025
β-strand308-30928
α-helix311-32111
β-strand325-32739
α-helix339-35012
β-strand353-354211
β-strand357112
α-helix358-3603
β-strand362112
β-strand366-367211
α-helix371-3733
β-strand375-37959
α-helix384-3863
α-helix387-3948
β-strand399-40139
α-helix404-4074
α-helix413-43220
α-helix437-44913
α-helix453-46210
Chains C, F, I and S: 4 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix19-224
α-helix23-3513
α-helix381
β-strand39-45713
β-strand52114
β-strand63114
β-strand68-70313
α-helix80-9314
β-strand98-105813
β-strand110-118913

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ribulose bisphosphate carboxylase (large chain)B, E, H, Lprotein475Spinacia oleraceaP00875 (AlphaFold model)
Ribulose bisphosphate carboxylase (small chain)C, F, I, Sprotein123Spinacia oleraceaQ43832 (AlphaFold model)
Sequence of entity 1 (B, E, H, L), FASTA
>1AA1_1 RIBULOSE BISPHOSPHATE CARBOXYLASE (LARGE CHAIN) (chains B, E, H, L)
MSPQTETKASVGFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAE
SSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSI
VGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGL
SAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYL
NATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAV
IDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDRSR
GIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVAN
RVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMDTV
Sequence of entity 2 (C, F, I, S), FASTA
>1AA1_2 RIBULOSE BISPHOSPHATE CARBOXYLASE (SMALL CHAIN) (chains C, F, I, S)
MQVWPILNLKKYETLSYLPPLTTDQLARQVDYLLNNKWVPCLEFETDHGFVYREHHNSPG
YYDGRYWTMWKLPMFGCTDPAQVLNELEECKKEYPNAFIRIIGFDSNREVQCISFIAYKP
AGY

Ligands and cofactors

IDNameFormulaCopies
3PG3-phosphoglyceric acidC3 H7 O7 P8
MGMagnesium ionMg4

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:

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