Current Protein Identity:Q8DIS5 New Search
Main Difference Dimensions in This Set
Different mutation/modification Different ligand/ion 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
2YBV STRUCTURE OF RUBISCO FROM THERMOSYNECHOCOCCUS ELONGATUS Deposited 2011-03-10 Assembly 1 Protein heterocomplex Heteromer;Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein count
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
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 A1 1–475(475 aa) Fragment:RbcL
Chain A2 1–475(475 aa) Fragment:RbcL
Chain A3 1–475(475 aa) Fragment:RbcL
Chain A4 1–475(475 aa) Fragment:RbcL
Chain A5 1–475(475 aa) Fragment:RbcL
Chain A6 1–475(475 aa) Fragment:RbcL
Chain A7 1–475(475 aa) Fragment:RbcL
Chain A8 1–475(475 aa) Fragment:RbcL
Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A 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 S1 1–475(475 aa) Fragment:RbcL
Chain S2 1–475(475 aa) Fragment:RbcL
Chain S3 1–475(475 aa) Fragment:RbcL
Chain S4 1–475(475 aa) Fragment:RbcL
Chain S5 1–475(475 aa) Fragment:RbcL
Chain S6 1–475(475 aa) Fragment:RbcL
Chain S7 1–475(475 aa) Fragment:RbcL
Chain S8 1–475(475 aa) Fragment:RbcL
Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A 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 C1 1–475(475 aa) Fragment:RbcL
Chain C2 1–475(475 aa) Fragment:RbcL
Chain C3 1–475(475 aa) Fragment:RbcL
Chain C4 1–475(475 aa) Fragment:RbcL
Chain C5 1–475(475 aa) Fragment:RbcL
Chain C6 1–475(475 aa) Fragment:RbcL
Chain C7 1–475(475 aa) Fragment:RbcL
Chain C8 1–475(475 aa) Fragment:RbcL
Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A 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 E1 1–475(475 aa) Fragment:RbcL
Chain E2 1–475(475 aa) Fragment:RbcL
Chain E3 1–475(475 aa) Fragment:RbcL
Chain E4 1–475(475 aa) Fragment:RbcL
Chain E5 1–475(475 aa) Fragment:RbcL
Chain E6 1–475(475 aa) Fragment:RbcL
Chain E7 1–475(475 aa) Fragment:RbcL
Chain E8 1–475(475 aa) Fragment:RbcL
Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A 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 G1 1–475(475 aa) Fragment:RbcL
Chain G2 1–475(475 aa) Fragment:RbcL
Chain G3 1–475(475 aa) Fragment:RbcL
Chain G4 1–475(475 aa) Fragment:RbcL
Chain G5 1–475(475 aa) Fragment:RbcL
Chain G6 1–475(475 aa) Fragment:RbcL
Chain G7 1–475(475 aa) Fragment:RbcL
Chain G8 1–475(475 aa) Fragment:RbcL
Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A 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 I1 1–475(475 aa) Fragment:RbcL
Chain I2 1–475(475 aa) Fragment:RbcL
Chain I3 1–475(475 aa) Fragment:RbcL
Chain I4 1–475(475 aa) Fragment:RbcL
Chain I5 1–475(475 aa) Fragment:RbcL
Chain I6 1–475(475 aa) Fragment:RbcL
Chain I7 1–475(475 aa) Fragment:RbcL
Chain I8 1–475(475 aa) Fragment:RbcL
Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A 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 K1 1–475(475 aa) Fragment:RbcL
Chain K2 1–475(475 aa) Fragment:RbcL
Chain K3 1–475(475 aa) Fragment:RbcL
Chain K4 1–475(475 aa) Fragment:RbcL
Chain K5 1–475(475 aa) Fragment:RbcL
Chain K6 1–475(475 aa) Fragment:RbcL
Chain K7 1–475(475 aa) Fragment:RbcL
Chain K8 1–475(475 aa) Fragment:RbcL
Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A 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 M1 1–475(475 aa) Fragment:RbcL
Chain M2 1–475(475 aa) Fragment:RbcL
Chain M3 1–475(475 aa) Fragment:RbcL
Chain M4 1–475(475 aa) Fragment:RbcL
Chain M5 1–475(475 aa) Fragment:RbcL
Chain M6 1–475(475 aa) Fragment:RbcL
Chain M7 1–475(475 aa) Fragment:RbcL
Chain M8 1–475(475 aa) Fragment:RbcL
Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A 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 O1 1–475(475 aa) Fragment:RbcL
Chain O2 1–475(475 aa) Fragment:RbcL
Chain O3 1–475(475 aa) Fragment:RbcL
Chain O4 1–475(475 aa) Fragment:RbcL
Chain O5 1–475(475 aa) Fragment:RbcL
Chain O6 1–475(475 aa) Fragment:RbcL
Chain O7 1–475(475 aa) Fragment:RbcL
Chain O8 1–475(475 aa) Fragment:RbcL
Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A 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 Q1 1–475(475 aa) Fragment:RbcL
Chain Q2 1–475(475 aa) Fragment:RbcL
Chain Q3 1–475(475 aa) Fragment:RbcL
Chain Q4 1–475(475 aa) Fragment:RbcL
Chain Q5 1–475(475 aa) Fragment:RbcL
Chain Q6 1–475(475 aa) Fragment:RbcL
Chain Q7 1–475(475 aa) Fragment:RbcL
Chain Q8 1–475(475 aa) Fragment:RbcL
Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A Mutation:F345I / P415A 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