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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：Q9SN73 New Search
5PDB entries
14Biological assembly
100chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
6EKB Crystal structure of the BSD2 homolog of Arabidopsis thaliana Deposited 2017-09-26 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 57–136（80 aa）
Mutation：K56M ZN ZINC ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；20 % PEG 10,000, 8 % ethylene glycol and 0.1 M HEPES-NaOH pH 7.5
Resolution 1.90 Å R-free 0.216
6EKC Crystal structure of the BSD2 homolog of Arabidopsis thaliana bound to the octameric assembly of RbcL from Thermosynechococcus elongatus Deposited 2017-09-26 Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
Chain B1 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain B2 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain B3 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain B4 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain B5 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain B6 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain B7 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain B8 57–136（80 aa） Fragment：mature protein, residues 53-136
Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M ZN ZINC ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；21 % PEG 3350 and 0.12M DL-malic acid pH 7.0
Resolution 2.63 Å R-free 0.274
6EKC Crystal structure of the BSD2 homolog of Arabidopsis thaliana bound to the octameric assembly of RbcL from Thermosynechococcus elongatus Deposited 2017-09-26 Assembly 10 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
Chain T1 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain T2 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain T3 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain T4 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain T5 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain T6 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain T7 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain T8 57–136（80 aa） Fragment：mature protein, residues 53-136
Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M ZN ZINC ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；21 % PEG 3350 and 0.12M DL-malic acid pH 7.0
Resolution 2.63 Å R-free 0.274
6EKC Crystal structure of the BSD2 homolog of Arabidopsis thaliana bound to the octameric assembly of RbcL from Thermosynechococcus elongatus Deposited 2017-09-26 Assembly 2 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
Chain D1 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain D2 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain D3 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain D4 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain D5 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain D6 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain D7 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain D8 57–136（80 aa） Fragment：mature protein, residues 53-136
Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M ZN ZINC ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；21 % PEG 3350 and 0.12M DL-malic acid pH 7.0
Resolution 2.63 Å R-free 0.274
6EKC Crystal structure of the BSD2 homolog of Arabidopsis thaliana bound to the octameric assembly of RbcL from Thermosynechococcus elongatus Deposited 2017-09-26 Assembly 3 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
Chain F1 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain F2 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain F3 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain F4 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain F5 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain F6 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain F7 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain F8 57–136（80 aa） Fragment：mature protein, residues 53-136
Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M ZN ZINC ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；21 % PEG 3350 and 0.12M DL-malic acid pH 7.0
Resolution 2.63 Å R-free 0.274
6EKC Crystal structure of the BSD2 homolog of Arabidopsis thaliana bound to the octameric assembly of RbcL from Thermosynechococcus elongatus Deposited 2017-09-26 Assembly 4 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
Chain H1 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain H2 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain H3 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain H4 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain H5 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain H6 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain H7 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain H8 57–136（80 aa） Fragment：mature protein, residues 53-136
Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M ZN ZINC ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；21 % PEG 3350 and 0.12M DL-malic acid pH 7.0
Resolution 2.63 Å R-free 0.274
6EKC Crystal structure of the BSD2 homolog of Arabidopsis thaliana bound to the octameric assembly of RbcL from Thermosynechococcus elongatus Deposited 2017-09-26 Assembly 5 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
Chain J1 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain J2 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain J3 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain J4 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain J5 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain J6 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain J7 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain J8 57–136（80 aa） Fragment：mature protein, residues 53-136
Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M ZN ZINC ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；21 % PEG 3350 and 0.12M DL-malic acid pH 7.0
Resolution 2.63 Å R-free 0.274
6EKC Crystal structure of the BSD2 homolog of Arabidopsis thaliana bound to the octameric assembly of RbcL from Thermosynechococcus elongatus Deposited 2017-09-26 Assembly 6 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
Chain L1 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain L2 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain L3 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain L4 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain L5 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain L6 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain L7 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain L8 57–136（80 aa） Fragment：mature protein, residues 53-136
Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M ZN ZINC ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；21 % PEG 3350 and 0.12M DL-malic acid pH 7.0
Resolution 2.63 Å R-free 0.274
6EKC Crystal structure of the BSD2 homolog of Arabidopsis thaliana bound to the octameric assembly of RbcL from Thermosynechococcus elongatus Deposited 2017-09-26 Assembly 7 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
Chain N1 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain N2 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain N3 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain N4 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain N5 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain N6 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain N7 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain N8 57–136（80 aa） Fragment：mature protein, residues 53-136
Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M ZN ZINC ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；21 % PEG 3350 and 0.12M DL-malic acid pH 7.0
Resolution 2.63 Å R-free 0.274
6EKC Crystal structure of the BSD2 homolog of Arabidopsis thaliana bound to the octameric assembly of RbcL from Thermosynechococcus elongatus Deposited 2017-09-26 Assembly 8 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
Chain P1 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain P2 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain P3 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain P4 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain P5 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain P6 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain P7 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain P8 57–136（80 aa） Fragment：mature protein, residues 53-136
Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M ZN ZINC ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；21 % PEG 3350 and 0.12M DL-malic acid pH 7.0
Resolution 2.63 Å R-free 0.274
6EKC Crystal structure of the BSD2 homolog of Arabidopsis thaliana bound to the octameric assembly of RbcL from Thermosynechococcus elongatus Deposited 2017-09-26 Assembly 9 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
Chain R1 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain R2 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain R3 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain R4 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain R5 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain R6 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain R7 57–136（80 aa） Fragment：mature protein, residues 53-136
Chain R8 57–136（80 aa） Fragment：mature protein, residues 53-136
Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M Mutation：K56M ZN ZINC ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；21 % PEG 3350 and 0.12M DL-malic acid pH 7.0
Resolution 2.63 Å R-free 0.274
8ILB The complexes of RbcL, AtRaf1 and AtBSD2 (LFB) Deposited 2023-03-03 Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric（18） Consistent with protein count
Chain F 57–136（80 aa）
Chain G 57–136（80 aa）
Chain H 57–136（80 aa）
Chain I 57–136（80 aa）
Chain O 57–136（80 aa）
Chain P 57–136（80 aa）
Chain Q 57–136（80 aa）
Chain R 57–136（80 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
8ILM The cryo-EM structure of eight Rubisco large subunits (RbcL), two Arabidopsis thaliana Rubisco accumulation factors 1 (AtRaf1), and seven Arabidopsis thaliana Bundle Sheath Defective 2 (AtBSD2) Deposited 2023-03-03 Assembly 1 Protein heterocomplex Heteromer；Protein × 19 PDB declaration: nonadecameric（19） Consistent with protein count
Chain C 57–136（80 aa）
Chain L 57–136（80 aa）
Chain M 57–136（80 aa）
Chain N 57–136（80 aa）
Chain O 57–136（80 aa）
Chain P 57–136（80 aa）
Chain Q 57–136（80 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9CI2 Anthoceros agrestis Rubisco octamer core complexed with small subunits and Arabidopsis thaliana BSD2 Deposited 2024-07-02 Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric（16） Consistent with protein count
Chain 1 1–136（136 aa）
Chain 2 1–136（136 aa）
Chain 3 1–136（136 aa）
Chain 4 1–136（136 aa）
Not recorded MG MAGNESIUM ION × 4 CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8；20 mM Tris pH 8.0 50 mM NaCl
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.