SAXSdb — 6ekc

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Ribulose bisphosphate carboxylase large chain

Thermosynechococcus elongatus (strain BP-1)

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain A1； UniProt 1–475 Chain A2； UniProt 1–475 Chain A3； UniProt 1–475 Chain A4； UniProt 1–475 Chain A5； UniProt 1–475 Chain A6； UniProt 1–475 Chain A7； UniProt 1–475 Chain A8； UniProt 1–475	Fragment：RbcL Mutation：F345I / P415A	DnaJ/Hsp40 cysteine-rich domain superfamily protein × 8 （Q9SN73） 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
10	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain S1； UniProt 1–475 Chain S2； UniProt 1–475 Chain S3； UniProt 1–475 Chain S4； UniProt 1–475 Chain S5； UniProt 1–475 Chain S6； UniProt 1–475 Chain S7； UniProt 1–475 Chain S8； UniProt 1–475	Fragment：RbcL Mutation：F345I / P415A	DnaJ/Hsp40 cysteine-rich domain superfamily protein × 8 （Q9SN73） 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
2	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain C1； UniProt 1–475 Chain C2； UniProt 1–475 Chain C3； UniProt 1–475 Chain C4； UniProt 1–475 Chain C5； UniProt 1–475 Chain C6； UniProt 1–475 Chain C7； UniProt 1–475 Chain C8； UniProt 1–475	Fragment：RbcL Mutation：F345I / P415A	DnaJ/Hsp40 cysteine-rich domain superfamily protein × 8 （Q9SN73） 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
3	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain E1； UniProt 1–475 Chain E2； UniProt 1–475 Chain E3； UniProt 1–475 Chain E4； UniProt 1–475 Chain E5； UniProt 1–475 Chain E6； UniProt 1–475 Chain E7； UniProt 1–475 Chain E8； UniProt 1–475	Fragment：RbcL Mutation：F345I / P415A	DnaJ/Hsp40 cysteine-rich domain superfamily protein × 8 （Q9SN73） 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
4	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain G1； UniProt 1–475 Chain G2； UniProt 1–475 Chain G3； UniProt 1–475 Chain G4； UniProt 1–475 Chain G5； UniProt 1–475 Chain G6； UniProt 1–475 Chain G7； UniProt 1–475 Chain G8； UniProt 1–475	Fragment：RbcL Mutation：F345I / P415A	DnaJ/Hsp40 cysteine-rich domain superfamily protein × 8 （Q9SN73） 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
5	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain I1； UniProt 1–475 Chain I2； UniProt 1–475 Chain I3； UniProt 1–475 Chain I4； UniProt 1–475 Chain I5； UniProt 1–475 Chain I6； UniProt 1–475 Chain I7； UniProt 1–475 Chain I8； UniProt 1–475	Fragment：RbcL Mutation：F345I / P415A	DnaJ/Hsp40 cysteine-rich domain superfamily protein × 8 （Q9SN73） 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
6	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain K1； UniProt 1–475 Chain K2； UniProt 1–475 Chain K3； UniProt 1–475 Chain K4； UniProt 1–475 Chain K5； UniProt 1–475 Chain K6； UniProt 1–475 Chain K7； UniProt 1–475 Chain K8； UniProt 1–475	Fragment：RbcL Mutation：F345I / P415A	DnaJ/Hsp40 cysteine-rich domain superfamily protein × 8 （Q9SN73） 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
7	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain M1； UniProt 1–475 Chain M2； UniProt 1–475 Chain M3； UniProt 1–475 Chain M4； UniProt 1–475 Chain M5； UniProt 1–475 Chain M6； UniProt 1–475 Chain M7； UniProt 1–475 Chain M8； UniProt 1–475	Fragment：RbcL Mutation：F345I / P415A	DnaJ/Hsp40 cysteine-rich domain superfamily protein × 8 （Q9SN73） 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
8	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain O1； UniProt 1–475 Chain O2； UniProt 1–475 Chain O3； UniProt 1–475 Chain O4； UniProt 1–475 Chain O5； UniProt 1–475 Chain O6； UniProt 1–475 Chain O7； UniProt 1–475 Chain O8； UniProt 1–475	Fragment：RbcL Mutation：F345I / P415A	DnaJ/Hsp40 cysteine-rich domain superfamily protein × 8 （Q9SN73） 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
9	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain Q1； UniProt 1–475 Chain Q2； UniProt 1–475 Chain Q3； UniProt 1–475 Chain Q4； UniProt 1–475 Chain Q5； UniProt 1–475 Chain Q6； UniProt 1–475 Chain Q7； UniProt 1–475 Chain Q8； UniProt 1–475	Fragment：RbcL Mutation：F345I / P415A	DnaJ/Hsp40 cysteine-rich domain superfamily protein × 8 （Q9SN73） 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

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 6EKC	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2YBV STRUCTURE OF RUBISCO FROM THERMOSYNECHOCOCCUS ELONGATUS Deposited 2011-03-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–475（475 aa） Chain C 1–475（475 aa） Chain E 1–475（475 aa） Chain G 1–475（475 aa） Chain I 1–475（475 aa） Chain K 1–475（475 aa） Chain M 1–475（475 aa） Chain O 1–475（475 aa）	Not recorded	CL CHLORIDE ION × 15	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；5% PEG8000, 20% PEG200, 10% GLYCEROL, 100MM HEPES, PH 7	Resolution 2.30 Å R-free 0.232
3ZXW STRUCTURE OF ACTIVATED RUBISCO FROM THERMOSYNECHOCOCCUS ELONGATUS COMPLEXED WITH 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE Deposited 2011-08-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–475（475 aa） Chain C 1–475（475 aa） Chain E 1–475（475 aa） Chain G 1–475（475 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	MG MAGNESIUM ION × 8 CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE × 8 GOL GLYCEROL × 22	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；80 MM HEPES, 20 MM MGCL2, 8% (W/V) PEG4000, 30% (V/V) GLYCEROL, PH=8	Resolution 2.10 Å R-free 0.213

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RBL_THEEB
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A1； PDBConstruct 1–475； UniProt 1–475 Author chain A2； PDBConstruct 1–475； UniProt 1–475 Author chain A3； PDBConstruct 1–475； UniProt 1–475 Author chain A4； PDBConstruct 1–475； UniProt 1–475 Author chain A5； PDBConstruct 1–475； UniProt 1–475 Author chain A6； PDBConstruct 1–475； UniProt 1–475 Author chain A7； PDBConstruct 1–475； UniProt 1–475 Author chain A8； PDBConstruct 1–475； UniProt 1–475 Author chain C1； PDBConstruct 1–475； UniProt 1–475 Author chain C2； PDBConstruct 1–475； UniProt 1–475 Author chain C3； PDBConstruct 1–475； UniProt 1–475 Author chain C4； PDBConstruct 1–475； UniProt 1–475 Author chain C5； PDBConstruct 1–475； UniProt 1–475 Author chain C6； PDBConstruct 1–475； UniProt 1–475 Author chain C7； PDBConstruct 1–475； UniProt 1–475 Author chain C8； PDBConstruct 1–475； UniProt 1–475 Author chain E1； PDBConstruct 1–475； UniProt 1–475 Author chain E2； PDBConstruct 1–475； UniProt 1–475 Author chain E3； PDBConstruct 1–475； UniProt 1–475 Author chain E4； PDBConstruct 1–475； UniProt 1–475 Author chain E5； PDBConstruct 1–475； UniProt 1–475 Author chain E6； PDBConstruct 1–475； UniProt 1–475 Author chain E7； PDBConstruct 1–475； UniProt 1–475 Author chain E8； PDBConstruct 1–475； UniProt 1–475 Author chain G1； PDBConstruct 1–475； UniProt 1–475 Author chain G2； PDBConstruct 1–475； UniProt 1–475 Author chain G3； PDBConstruct 1–475； UniProt 1–475 Author chain G4； PDBConstruct 1–475； UniProt 1–475 Author chain G5； PDBConstruct 1–475； UniProt 1–475 Author chain G6； PDBConstruct 1–475； UniProt 1–475 Author chain G7； PDBConstruct 1–475； UniProt 1–475 Author chain G8； PDBConstruct 1–475； UniProt 1–475 Author chain I1； PDBConstruct 1–475； UniProt 1–475 Author chain I2； PDBConstruct 1–475； UniProt 1–475 Author chain I3； PDBConstruct 1–475； UniProt 1–475 Author chain I4； PDBConstruct 1–475； UniProt 1–475 Author chain I5； PDBConstruct 1–475； UniProt 1–475 Author chain I6； PDBConstruct 1–475； UniProt 1–475 Author chain I7； PDBConstruct 1–475； UniProt 1–475 Author chain I8； PDBConstruct 1–475； UniProt 1–475 Author chain K1； PDBConstruct 1–475； UniProt 1–475 Author chain K2； PDBConstruct 1–475； UniProt 1–475 Author chain K3； PDBConstruct 1–475； UniProt 1–475 Author chain K4； PDBConstruct 1–475； UniProt 1–475 Author chain K5； PDBConstruct 1–475； UniProt 1–475 Author chain K6； PDBConstruct 1–475； UniProt 1–475 Author chain K7； PDBConstruct 1–475； UniProt 1–475 Author chain K8； PDBConstruct 1–475； UniProt 1–475 Author chain M1； PDBConstruct 1–475； UniProt 1–475 Author chain M2； PDBConstruct 1–475； UniProt 1–475 Author chain M3； PDBConstruct 1–475； UniProt 1–475 Author chain M4； PDBConstruct 1–475； UniProt 1–475 Author chain M5； PDBConstruct 1–475； UniProt 1–475 Author chain M6； PDBConstruct 1–475； UniProt 1–475 Author chain M7； PDBConstruct 1–475； UniProt 1–475 Author chain M8； PDBConstruct 1–475； UniProt 1–475 Author chain O1； PDBConstruct 1–475； UniProt 1–475 Author chain O2； PDBConstruct 1–475； UniProt 1–475 Author chain O3； PDBConstruct 1–475； UniProt 1–475 Author chain O4； PDBConstruct 1–475； UniProt 1–475 Author chain O5； PDBConstruct 1–475； UniProt 1–475 Author chain O6； PDBConstruct 1–475； UniProt 1–475 Author chain O7； PDBConstruct 1–475； UniProt 1–475 Author chain O8； PDBConstruct 1–475； UniProt 1–475 Author chain Q1； PDBConstruct 1–475； UniProt 1–475 Author chain Q2； PDBConstruct 1–475； UniProt 1–475 Author chain Q3； PDBConstruct 1–475； UniProt 1–475 Author chain Q4； PDBConstruct 1–475； UniProt 1–475 Author chain Q5； PDBConstruct 1–475； UniProt 1–475 Author chain Q6； PDBConstruct 1–475； UniProt 1–475 Author chain Q7； PDBConstruct 1–475； UniProt 1–475 Author chain Q8； PDBConstruct 1–475； UniProt 1–475 Author chain S1； PDBConstruct 1–475； UniProt 1–475 Author chain S2； PDBConstruct 1–475； UniProt 1–475 Author chain S3； PDBConstruct 1–475； UniProt 1–475 Author chain S4； PDBConstruct 1–475； UniProt 1–475 Author chain S5； PDBConstruct 1–475； UniProt 1–475 Author chain S6； PDBConstruct 1–475； UniProt 1–475 Author chain S7； PDBConstruct 1–475； UniProt 1–475 Author chain S8； PDBConstruct 1–475； UniProt 1–475

DnaJ/Hsp40 cysteine-rich domain superfamily protein

Arabidopsis thaliana

UniProt Q9SN73

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain B1； UniProt 57–136 Chain B2； UniProt 57–136 Chain B3； UniProt 57–136 Chain B4； UniProt 57–136 Chain B5； UniProt 57–136 Chain B6； UniProt 57–136 Chain B7； UniProt 57–136 Chain B8； UniProt 57–136	Fragment：mature protein, residues 53-136 Mutation：K56M	Ribulose bisphosphate carboxylase large chain × 8 （Q8DIS5） 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
10	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain T1； UniProt 57–136 Chain T2； UniProt 57–136 Chain T3； UniProt 57–136 Chain T4； UniProt 57–136 Chain T5； UniProt 57–136 Chain T6； UniProt 57–136 Chain T7； UniProt 57–136 Chain T8； UniProt 57–136	Fragment：mature protein, residues 53-136 Mutation：K56M	Ribulose bisphosphate carboxylase large chain × 8 （Q8DIS5） 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
2	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain D1； UniProt 57–136 Chain D2； UniProt 57–136 Chain D3； UniProt 57–136 Chain D4； UniProt 57–136 Chain D5； UniProt 57–136 Chain D6； UniProt 57–136 Chain D7； UniProt 57–136 Chain D8； UniProt 57–136	Fragment：mature protein, residues 53-136 Mutation：K56M	Ribulose bisphosphate carboxylase large chain × 8 （Q8DIS5） 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
3	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain F1； UniProt 57–136 Chain F2； UniProt 57–136 Chain F3； UniProt 57–136 Chain F4； UniProt 57–136 Chain F5； UniProt 57–136 Chain F6； UniProt 57–136 Chain F7； UniProt 57–136 Chain F8； UniProt 57–136	Fragment：mature protein, residues 53-136 Mutation：K56M	Ribulose bisphosphate carboxylase large chain × 8 （Q8DIS5） 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
4	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain H1； UniProt 57–136 Chain H2； UniProt 57–136 Chain H3； UniProt 57–136 Chain H4； UniProt 57–136 Chain H5； UniProt 57–136 Chain H6； UniProt 57–136 Chain H7； UniProt 57–136 Chain H8； UniProt 57–136	Fragment：mature protein, residues 53-136 Mutation：K56M	Ribulose bisphosphate carboxylase large chain × 8 （Q8DIS5） 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
5	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain J1； UniProt 57–136 Chain J2； UniProt 57–136 Chain J3； UniProt 57–136 Chain J4； UniProt 57–136 Chain J5； UniProt 57–136 Chain J6； UniProt 57–136 Chain J7； UniProt 57–136 Chain J8； UniProt 57–136	Fragment：mature protein, residues 53-136 Mutation：K56M	Ribulose bisphosphate carboxylase large chain × 8 （Q8DIS5） 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
6	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain L1； UniProt 57–136 Chain L2； UniProt 57–136 Chain L3； UniProt 57–136 Chain L4； UniProt 57–136 Chain L5； UniProt 57–136 Chain L6； UniProt 57–136 Chain L7； UniProt 57–136 Chain L8； UniProt 57–136	Fragment：mature protein, residues 53-136 Mutation：K56M	Ribulose bisphosphate carboxylase large chain × 8 （Q8DIS5） 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
7	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain N1； UniProt 57–136 Chain N2； UniProt 57–136 Chain N3； UniProt 57–136 Chain N4； UniProt 57–136 Chain N5； UniProt 57–136 Chain N6； UniProt 57–136 Chain N7； UniProt 57–136 Chain N8； UniProt 57–136	Fragment：mature protein, residues 53-136 Mutation：K56M	Ribulose bisphosphate carboxylase large chain × 8 （Q8DIS5） 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
8	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain P1； UniProt 57–136 Chain P2； UniProt 57–136 Chain P3； UniProt 57–136 Chain P4； UniProt 57–136 Chain P5； UniProt 57–136 Chain P6； UniProt 57–136 Chain P7； UniProt 57–136 Chain P8； UniProt 57–136	Fragment：mature protein, residues 53-136 Mutation：K56M	Ribulose bisphosphate carboxylase large chain × 8 （Q8DIS5） 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
9	Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain R1； UniProt 57–136 Chain R2； UniProt 57–136 Chain R3； UniProt 57–136 Chain R4； UniProt 57–136 Chain R5； UniProt 57–136 Chain R6； UniProt 57–136 Chain R7； UniProt 57–136 Chain R8； UniProt 57–136	Fragment：mature protein, residues 53-136 Mutation：K56M	Ribulose bisphosphate carboxylase large chain × 8 （Q8DIS5） 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

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 6EKC	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6EKB Crystal structure of the BSD2 homolog of Arabidopsis thaliana Deposited 2017-09-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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
8ILB The complexes of RbcL, AtRaf1 and AtBSD2 (LFB) Deposited 2023-03-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 19 PDB declaration: nonadecameric	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	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric	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

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q9SN73_ARATH
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B1； PDBConstruct 2–81； UniProt 57–136 Author chain B2； PDBConstruct 2–81； UniProt 57–136 Author chain B3； PDBConstruct 2–81； UniProt 57–136 Author chain B4； PDBConstruct 2–81； UniProt 57–136 Author chain B5； PDBConstruct 2–81； UniProt 57–136 Author chain B6； PDBConstruct 2–81； UniProt 57–136 Author chain B7； PDBConstruct 2–81； UniProt 57–136 Author chain B8； PDBConstruct 2–81； UniProt 57–136 Author chain D1； PDBConstruct 2–81； UniProt 57–136 Author chain D2； PDBConstruct 2–81； UniProt 57–136 Author chain D3； PDBConstruct 2–81； UniProt 57–136 Author chain D4； PDBConstruct 2–81； UniProt 57–136 Author chain D5； PDBConstruct 2–81； UniProt 57–136 Author chain D6； PDBConstruct 2–81； UniProt 57–136 Author chain D7； PDBConstruct 2–81； UniProt 57–136 Author chain D8； PDBConstruct 2–81； UniProt 57–136 Author chain F1； PDBConstruct 2–81； UniProt 57–136 Author chain F2； PDBConstruct 2–81； UniProt 57–136 Author chain F3； PDBConstruct 2–81； UniProt 57–136 Author chain F4； PDBConstruct 2–81； UniProt 57–136 Author chain F5； PDBConstruct 2–81； UniProt 57–136 Author chain F6； PDBConstruct 2–81； UniProt 57–136 Author chain F7； PDBConstruct 2–81； UniProt 57–136 Author chain F8； PDBConstruct 2–81； UniProt 57–136 Author chain H1； PDBConstruct 2–81； UniProt 57–136 Author chain H2； PDBConstruct 2–81； UniProt 57–136 Author chain H3； PDBConstruct 2–81； UniProt 57–136 Author chain H4； PDBConstruct 2–81； UniProt 57–136 Author chain H5； PDBConstruct 2–81； UniProt 57–136 Author chain H6； PDBConstruct 2–81； UniProt 57–136 Author chain H7； PDBConstruct 2–81； UniProt 57–136 Author chain H8； PDBConstruct 2–81； UniProt 57–136 Author chain J1； PDBConstruct 2–81； UniProt 57–136 Author chain J2； PDBConstruct 2–81； UniProt 57–136 Author chain J3； PDBConstruct 2–81； UniProt 57–136 Author chain J4； PDBConstruct 2–81； UniProt 57–136 Author chain J5； PDBConstruct 2–81； UniProt 57–136 Author chain J6； PDBConstruct 2–81； UniProt 57–136 Author chain J7； PDBConstruct 2–81； UniProt 57–136 Author chain J8； PDBConstruct 2–81； UniProt 57–136 Author chain L1； PDBConstruct 2–81； UniProt 57–136 Author chain L2； PDBConstruct 2–81； UniProt 57–136 Author chain L3； PDBConstruct 2–81； UniProt 57–136 Author chain L4； PDBConstruct 2–81； UniProt 57–136 Author chain L5； PDBConstruct 2–81； UniProt 57–136 Author chain L6； PDBConstruct 2–81； UniProt 57–136 Author chain L7； PDBConstruct 2–81； UniProt 57–136 Author chain L8； PDBConstruct 2–81； UniProt 57–136 Author chain N1； PDBConstruct 2–81； UniProt 57–136 Author chain N2； PDBConstruct 2–81； UniProt 57–136 Author chain N3； PDBConstruct 2–81； UniProt 57–136 Author chain N4； PDBConstruct 2–81； UniProt 57–136 Author chain N5； PDBConstruct 2–81； UniProt 57–136 Author chain N6； PDBConstruct 2–81； UniProt 57–136 Author chain N7； PDBConstruct 2–81； UniProt 57–136 Author chain N8； PDBConstruct 2–81； UniProt 57–136 Author chain P1； PDBConstruct 2–81； UniProt 57–136 Author chain P2； PDBConstruct 2–81； UniProt 57–136 Author chain P3； PDBConstruct 2–81； UniProt 57–136 Author chain P4； PDBConstruct 2–81； UniProt 57–136 Author chain P5； PDBConstruct 2–81； UniProt 57–136 Author chain P6； PDBConstruct 2–81； UniProt 57–136 Author chain P7； PDBConstruct 2–81； UniProt 57–136 Author chain P8； PDBConstruct 2–81； UniProt 57–136 Author chain R1； PDBConstruct 2–81； UniProt 57–136 Author chain R2； PDBConstruct 2–81； UniProt 57–136 Author chain R3； PDBConstruct 2–81； UniProt 57–136 Author chain R4； PDBConstruct 2–81； UniProt 57–136 Author chain R5； PDBConstruct 2–81； UniProt 57–136 Author chain R6； PDBConstruct 2–81； UniProt 57–136 Author chain R7； PDBConstruct 2–81； UniProt 57–136 Author chain R8； PDBConstruct 2–81； UniProt 57–136 Author chain T1； PDBConstruct 2–81； UniProt 57–136 Author chain T2； PDBConstruct 2–81； UniProt 57–136 Author chain T3； PDBConstruct 2–81； UniProt 57–136 Author chain T4； PDBConstruct 2–81； UniProt 57–136 Author chain T5； PDBConstruct 2–81； UniProt 57–136 Author chain T6； PDBConstruct 2–81； UniProt 57–136 Author chain T7； PDBConstruct 2–81； UniProt 57–136 Author chain T8； PDBConstruct 2–81； UniProt 57–136

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6ekc
Deposition date deposition_date	2017-09-26
Structure title title	Crystal structure of the BSD2 homolog of Arabidopsis thaliana bound to the octameric assembly of RbcL from Thermosynechococcus elongatus
Keywords keywords	zinc finger, assembly chaperone, assembly intermediate, CHAPERONE; CHAPERONE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	— Å
Radius of gyration Rg (electron density) rg_electron	122.20 Å
Forward intensity I(0) i0	294776000000.00
Molecular weight molecular_weight	4579700.0 kDa
Excluded volume excluded_volume	5693900 Å³
Envelope volume envelope_volume	9168600 Å³
Hydration-shell volume shell_volume	602880 Å³
Envelope diameter envelope_diameter	446.1 Å
Shell Rg shell_rg	127.70 Å
Envelope Rg envelope_rg	118.50 Å
Shape Rg shape_rg	122.20 Å
Total Rg total_rg	122.30 Å
Total atoms total_atoms	321186
Residues n_residues	41600
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	324.0 Å
Rg (real space) rg_real	117.40 Å
Rg uncertainty (real space) rg_real_error	0.81 Å
I(0) (real space) i0_real	2.8040e+11
I(0) uncertainty (real space) i0_real_error	5.2020e+09
Rg (reciprocal space) rg_reciprocal	123.80 Å
I(0) (reciprocal space) i0_reciprocal	296000000000.0000
Solution quality estimate total_estimate	0.9115
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	149.5 Å
Skewness Skewness skewness	0.178
Kurtosis Kurtosis kurtosis	-0.451
Angular range angular_range	— – 0.0650 Å⁻¹
Current regularization parameter α current_alpha	0.9056
Highest regularization parameter α highest_alpha	12160000000.0000
Real-space data points n_real_points	14
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.005; Oscil: 0.989; Stabil: 0.963; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Ribulose bisphosphate carboxylase large chain
Molecular weight formula_weight	53031.3 kDa
EC 编号 ec_number	4.1.1.39
Mutation mutation	F345I / P415A
Source method src_method	man
Copy count entity_count	80

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	;A1,A2,A3,A4,A5,A6,A7,A8,C1,C2,C3,C4,C5,C6,C7,C8,E1,E2,E3,E4,E5,E6,E7,E8,G1,G2,G3,G4,G5,G6,G7,G8,I1,I2,I3,I4,I5,I6,I7,I8,K1,K2,K3,K4,K5,K6,K7,K8,M1,M2,M3,M4,M5,M6,M7,M8,O1,O2,O3,O4,O5,O6,O7,O8,Q1,Q2,Q3,Q4,Q5,Q6,Q7,Q8,S1,S2,S3,S4,S5,S6,S7,S8 ;
Atom count atom_count	321799

MAYTQSKSQKVGYQAGVKDYRLTYYTPDYTPKDTDILAAFRVTPQPGVPFEEAAAAVAAESSTGTWTTVWTDLLTDLDRYKGCCYDIEPLPGEDNQFIAYIAYPLDLFEEGSVTNMLTSIVGNVFGFKALKALRLEDLRIPVAYLKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSQPFQRWRDRFLFVADAIHKAQAETGEIKGHYLNVTAPTCEEMLKRAEFAKELEMPIIMHDFLTAGFTANTTLSKWCRDNGMLLHIHRAMHAVMDRQKNHGIHFRVLAKCLRMSGGDHIHTGTVVGKLEGDKAVTLGIVDLLRENYIEQDRSRGIYFTQDWASMPGVMAVASGGIHVWHMPALVDIFGDDAVLQFGGGTLGHPWGNAAGATANRVALEACIQARNEGRDLMREGGDIIREAARWSPELAAACELWKEIKFEFEAQDTI

来源 Source

来源生物 organism	Thermosynechococcus elongatus (strain BP-1)
NCBI Class编号 ncbi_taxonomy_id	197221
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	DnaJ/Hsp40 cysteine-rich domain superfamily protein
Molecular weight formula_weight	8355.5 kDa
Mutation mutation	K56M
Source method src_method	man
Copy count entity_count	80

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	;B1,B2,B3,B4,B5,B6,B7,B8,D1,D2,D3,D4,D5,D6,D7,D8,F1,F2,F3,F4,F5,F6,F7,F8,H1,H2,H3,H4,H5,H6,H7,H8,J1,J2,J3,J4,J5,J6,J7,J8,L1,L2,L3,L4,L5,L6,L7,L8,N1,N2,N3,N4,N5,N6,N7,N8,P1,P2,P3,P4,P5,P6,P7,P8,R1,R2,R3,R4,R5,R6,R7,R8,T1,T2,T3,T4,T5,T6,T7,T8 ;

MAANNNPQGTKPNSLVCANCEGEGCVACSQCKGGGVNLIDHFNGQFKAGALCWLCRGKKEVLCGDCNGAGFIGGFLSTFDE

来源 Source

来源生物 organism	Arabidopsis thaliana
通用名 common_name	Mouse-ear cress
NCBI Class编号 ncbi_taxonomy_id	3702
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	160

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	613

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8. Citations (1)

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Unit-cell length a length_a	217.918 Å
Unit-cell length b length_b	218.592 Å
Unit-cell length c length_c	310.273 Å
Unit-cell angle α angle_alpha	69.40 °
Unit-cell angle β angle_beta	81.51 °
Unit-cell angle γ angle_gamma	65.50 °
Molecules per unit cell Z z_pdb	80

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.630 Å
Low-resolution limit resolution_low	50.010 Å
R factor r_factor	0.2375
R_work r_work	0.2355
R_free r_free	0.2742

fit	/app/data/saxs_computation/ek/6ekc/6ekc.fit
pddf	/app/data/pr_computation/ek/6ekc/6ekc.pr.out
profile	/app/data/saxs_computation/ek/6ekc/6ekc.dat

Crystal structure of the BSD2 homolog of Arabidopsis thaliana bound to the octameric assembly of RbcL from Thermosynechococcus elongatus

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ribulose bisphosphate carboxylase large chain

State in the Current Structure

Other States of the Same Protein in the Database

DnaJ/Hsp40 cysteine-rich domain superfamily protein

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)