60 kDa chaperonin
Escherichia coli
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 homooligomer Homooligomer Protein × 14 PDB declaration: tetradecameric（14） Consistent with protein copy count | Chain A； UniProt 1–548 Chain B； UniProt 1–548 Chain C； UniProt 1–548 Chain D； UniProt 1–548 Chain E； UniProt 1–548 Chain F； UniProt 1–548 Chain G； UniProt 1–548 Chain H； UniProt 1–548 Chain I； UniProt 1–548 Chain J； UniProt 1–548 Chain K； UniProt 1–548 Chain L； UniProt 1–548 Chain M； UniProt 1–548 Chain N； UniProt 1–548 | Mutation：K105A | No other associated polymer | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；PEG 4000, HEPES | Resolution 3.04 Å R-free 0.256 |
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 4WSC | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1AON CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/(ADP)7 Deposited 1997-07-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric |
Chain A
2–548（547 aa）
Chain B
2–548（547 aa）
Chain C
2–548（547 aa）
Chain D
2–548（547 aa）
Chain E
2–548（547 aa）
Chain F
2–548（547 aa）
Chain G
2–548（547 aa）
Chain H
2–548（547 aa）
Chain I
2–548（547 aa）
Chain J
2–548（547 aa）
Chain K
2–548（547 aa）
Chain L
2–548（547 aa）
Chain M
2–548（547 aa）
Chain N
2–548（547 aa）
|
Not recorded | MG MAGNESIUM ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 7 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 5.5；PROTEIN WAS CRYSTALLIZED FROM 12% PEG3000, 0.25M SODIUM GLUTAMATE, 100MM CACODYLIC ACID, PH 5.5
|
Resolution 3.00 Å R-free 0.291 |
| 1DK7 CRYSTAL STRUCTURE OF AN ISOLATED APICAL DOMAIN OF GROEL Deposited 1999-12-06 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
191–336（146 aa）
Fragment：APICAL DOMAIN
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；292.3 K；PEG4K, LI2SO4, TRISHCL, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 19.3K
|
Resolution 2.02 Å R-free 0.241 |
| 1DK7 CRYSTAL STRUCTURE OF AN ISOLATED APICAL DOMAIN OF GROEL Deposited 1999-12-06 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
191–336（146 aa）
Fragment：APICAL DOMAIN
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；292.3 K；PEG4K, LI2SO4, TRISHCL, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 19.3K
|
Resolution 2.02 Å R-free 0.241 |
| 1DKD CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX Deposited 1999-12-07 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
191–336（146 aa）
Fragment：APICAL DOMAIN
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；PEG4K, MgCl2, TrisCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 18K
|
Resolution 2.10 Å R-free 0.264 |
| 1DKD CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX Deposited 1999-12-07 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
191–336（146 aa）
Fragment：APICAL DOMAIN
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；PEG4K, MgCl2, TrisCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 18K
|
Resolution 2.10 Å R-free 0.264 |
| 1DKD CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX Deposited 1999-12-07 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain C
191–336（146 aa）
Fragment：APICAL DOMAIN
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；PEG4K, MgCl2, TrisCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 18K
|
Resolution 2.10 Å R-free 0.264 |
| 1DKD CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX Deposited 1999-12-07 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain D
191–336（146 aa）
Fragment：APICAL DOMAIN
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；PEG4K, MgCl2, TrisCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 18K
|
Resolution 2.10 Å R-free 0.264 |
| 1DKD CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX Deposited 1999-12-07 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 5 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain A
191–336（146 aa）
Fragment：APICAL DOMAIN
Chain C
191–336（146 aa）
Fragment：APICAL DOMAIN
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；PEG4K, MgCl2, TrisCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 18K
|
Resolution 2.10 Å R-free 0.264 |
| 1DKD CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX Deposited 1999-12-07 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 6 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain B
191–336（146 aa）
Fragment：APICAL DOMAIN
Chain D
191–336（146 aa）
Fragment：APICAL DOMAIN
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；PEG4K, MgCl2, TrisCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 18K
|
Resolution 2.10 Å R-free 0.264 |
| 1FY9 CRYSTAL STRUCTURE OF THE HEXA-SUBSTITUTED MUTANT OF THE MOLECULAR CHAPERONIN GROEL APICAL DOMAIN Deposited 2000-09-28 | 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
184–376（193 aa）
Fragment：APICAL DOMAIN (RESIDUES 191-376)
|
Mutation：A212E/A223V/M233L/I305L/E308K/N326T | GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；290 K；0.75-0.9M POTASSIUM TARTRATE, 50MM MES SODIUM, pH 6.50, VAPOR DIFFUSION, HANGING DROP, temperature 290K
|
Resolution 2.20 Å R-free 0.292 |
| 1FYA CRYSTAL STRUCTURE OF THE HEXA-SUBSTITUTED MUTANT OF THE MOLECULAR CHAPERONIN GROEL APICAL DOMAIN Deposited 2000-09-28 | 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
184–376（193 aa）
Fragment：APICAL DOMAIN (RESIDUES 191-376)
|
Mutation：A212E/A223T/M233L/I305L/E308K/N326T | GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；290 K；0.75-0.9 M SODIUM POTASSIUM TARTRATE, 50 MM MES SODIUM, pH 6.50, VAPOR DIFFUSION, HANGING DROP, temperature 290K
|
Resolution 2.20 Å R-free 0.279 |
| 1JON GROEL (HSP60 CLASS) FRAGMENT COMPRISING RESIDUES 191-345 Deposited 1996-05-30 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
190–344（155 aa）
Fragment：POLYPEPTIDE BINDING (APICAL) DOMAIN, RESIDUES 191 - 345
|
Mutation：A262L, I267M | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8.5；290 K；11% PEG 4000, 50 MM TRIS-HCL, PH 8.5, 200 MM LISO4, 23 MG/ML PROTEIN, 17 DEG. C., temperature 290K
|
Resolution 2.50 Å R-free 0.287 |
| 1KID GROEL (HSP60 CLASS) FRAGMENT (APICAL DOMAIN) COMPRISING RESIDUES 191-376, MUTANT WITH ALA 262 REPLACED WITH LEU AND ILE 267 REPLACED WITH MET Deposited 1996-12-13 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
181–375（195 aa）
Fragment：APICAL DOMAIN, RESIDUES 191 - 376
|
Mutation：A262L, I267M | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8.5；pH 8.5
|
Resolution 1.70 Å R-free 0.224 |
| 1KP8 Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution Deposited 2001-12-30 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–547（547 aa）
Chain B
1–547（547 aa）
Chain C
1–547（547 aa）
Chain D
1–547（547 aa）
Chain E
1–547（547 aa）
Chain F
1–547（547 aa）
Chain G
1–547（547 aa）
Chain H
1–547（547 aa）
Chain I
1–547（547 aa）
Chain J
1–547（547 aa）
Chain K
1–547（547 aa）
Chain L
1–547（547 aa）
Chain M
1–547（547 aa）
Chain N
1–547（547 aa）
|
Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V | SO4 SULFATE ION × 22 MG MAGNESIUM ION × 14 K POTASSIUM ION × 16 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 14 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å R-free 0.258 |
| 1LA1 Gro-EL Fragment (Apical Domain) Comprising Residues 188-379 Deposited 2002-03-27 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
188–379（192 aa）
Fragment：Apical Domain
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；0.6 M NaCl, 14 % (w/v) PEG 6000, 100 mM Tris/HCl pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
|
Resolution 2.06 Å R-free 0.257 |
| 1MNF Domain motions in GroEL upon binding of an oligopeptide Deposited 2002-09-05 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 28 PDB declaration: 28-meric |
Chain A
1–547（547 aa）
Chain B
1–547（547 aa）
Chain C
1–547（547 aa）
Chain D
1–547（547 aa）
Chain E
1–547（547 aa）
Chain F
1–547（547 aa）
Chain G
1–547（547 aa）
Chain H
1–547（547 aa）
Chain I
1–547（547 aa）
Chain J
1–547（547 aa）
Chain K
1–547（547 aa）
Chain L
1–547（547 aa）
Chain M
1–547（547 aa）
Chain N
1–547（547 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 7；300 K；PEG, pH 7, VAPOR DIFFUSION, temperature 300K
|
Resolution 3.00 Å R-free 0.259 |
| 1OEL CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION Deposited 1995-11-21 | Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–547（547 aa）
Chain B
1–547（547 aa）
Chain C
1–547（547 aa）
Chain D
1–547（547 aa）
Chain E
1–547（547 aa）
Chain F
1–547（547 aa）
Chain G
1–547（547 aa）
|
Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V Mutation：R13G, A126V | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.80 Å R-free 0.270 |
| 1PCQ Crystal structure of groEL-groES Deposited 2003-05-16 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric |
Chain A
1–524（524 aa）
Chain B
1–524（524 aa）
Chain C
1–524（524 aa）
Chain D
1–524（524 aa）
Chain E
1–524（524 aa）
Chain F
1–524（524 aa）
Chain G
1–524（524 aa）
Chain H
1–524（524 aa）
Chain I
1–524（524 aa）
Chain J
1–524（524 aa）
Chain K
1–524（524 aa）
Chain L
1–524（524 aa）
Chain M
1–524（524 aa）
Chain N
1–524（524 aa）
|
Not recorded | MG MAGNESIUM ION × 7 K POTASSIUM ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 7 AF3 ALUMINUM FLUORIDE × 7 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.81 Å R-free 0.278 |
| 1SS8 GroEL Deposited 2004-03-23 | Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–524（524 aa）
Chain B
1–524（524 aa）
Chain C
1–524（524 aa）
Chain D
1–524（524 aa）
Chain E
1–524（524 aa）
Chain F
1–524（524 aa）
Chain G
1–524（524 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
EVAPORATION, RECRYSTALLIZATION；pH 8；298 K；PEG 8000, 1.72 M ammonium slufate, 4 mM CaCl2, 100mM Tris-acetate , pH 8.0, EVAPORATION, RECRYSTALLIZATION, temperature 298K
|
Resolution 2.70 Å R-free 0.249 |
| 1SS8 GroEL Deposited 2004-03-23 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric |
Chain A
1–524（524 aa）
Chain B
1–524（524 aa）
Chain C
1–524（524 aa）
Chain D
1–524（524 aa）
Chain E
1–524（524 aa）
Chain F
1–524（524 aa）
Chain G
1–524（524 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
EVAPORATION, RECRYSTALLIZATION；pH 8；298 K；PEG 8000, 1.72 M ammonium slufate, 4 mM CaCl2, 100mM Tris-acetate , pH 8.0, EVAPORATION, RECRYSTALLIZATION, temperature 298K
|
Resolution 2.70 Å R-free 0.249 |
| 1SVT Crystal structure of GroEL14-GroES7-(ADP-AlFx)7 Deposited 2004-03-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric |
Chain A
1–524（524 aa）
Chain B
1–524（524 aa）
Chain C
1–524（524 aa）
Chain D
1–524（524 aa）
Chain E
1–524（524 aa）
Chain F
1–524（524 aa）
Chain G
1–524（524 aa）
Chain H
1–524（524 aa）
Chain I
1–524（524 aa）
Chain J
1–524（524 aa）
Chain K
1–524（524 aa）
Chain L
1–524（524 aa）
Chain M
1–524（524 aa）
Chain N
1–524（524 aa）
|
Not recorded | MG MAGNESIUM ION × 7 K POTASSIUM ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 7 AF3 ALUMINUM FLUORIDE × 7 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；PEG3000, cacodylic acid, potassium chloride, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.81 Å R-free 0.274 |
| 1SX3 GroEL14-(ATPgammaS)14 Deposited 2004-03-30 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–525（525 aa）
Chain B
1–525（525 aa）
Chain C
1–525（525 aa）
Chain D
1–525（525 aa）
Chain E
1–525（525 aa）
Chain F
1–525（525 aa）
Chain G
1–525（525 aa）
Chain H
1–525（525 aa）
Chain I
1–525（525 aa）
Chain J
1–525（525 aa）
Chain K
1–525（525 aa）
Chain L
1–525（525 aa）
Chain M
1–525（525 aa）
Chain N
1–525（525 aa）
|
Not recorded | MG MAGNESIUM ION × 14 K POTASSIUM ION × 16 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 14 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；PEG 8000, bis-tris propane, ethylene glycol, glycerol, potassium chloride, calcium chloride, ATPgammaS, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.00 Å R-free 0.265 |
| 1SX4 GroEL-GroES-ADP7 Deposited 2004-03-30 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric |
Chain A
1–524（524 aa）
Chain B
1–524（524 aa）
Chain C
1–524（524 aa）
Chain D
1–524（524 aa）
Chain E
1–524（524 aa）
Chain F
1–524（524 aa）
Chain G
1–524（524 aa）
Chain H
1–524（524 aa）
Chain I
1–524（524 aa）
Chain J
1–524（524 aa）
Chain K
1–524（524 aa）
Chain L
1–524（524 aa）
Chain M
1–524（524 aa）
Chain N
1–524（524 aa）
|
Not recorded | MG MAGNESIUM ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 7 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；PEG 3000, cacodylic acid, sodium glutamate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 3.00 Å R-free 0.287 |
| 2C7C FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180) Deposited 2005-11-22 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric |
Chain A
1–547（547 aa）
Chain B
1–547（547 aa）
Chain C
1–547（547 aa）
Chain D
1–547（547 aa）
Chain E
1–547（547 aa）
Chain F
1–547（547 aa）
Chain G
1–547（547 aa）
Chain H
1–547（547 aa）
Chain I
1–547（547 aa）
Chain J
1–547（547 aa）
Chain K
1–547（547 aa）
Chain L
1–547（547 aa）
Chain M
1–547（547 aa）
Chain N
1–547（547 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
12.5MM HEPES, 5MM KCL, 5MM MGCL2；pH 7.5；12.5MM HEPES, 5MM KCL, 5MM MGCL2
cryo-EM vitrification conditions
Cryogen ETHANE；LIQUID ETHANE
|
Resolution 7.70 Å |
| 2C7D Fitted coordinates for GroEL-ADP7-GroES Cryo-EM complex (EMD-1181) Deposited 2005-11-22 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric |
Chain A
1–547（547 aa）
Chain B
1–547（547 aa）
Chain C
1–547（547 aa）
Chain D
1–547（547 aa）
Chain E
1–547（547 aa）
Chain F
1–547（547 aa）
Chain G
1–547（547 aa）
Chain H
1–547（547 aa）
Chain I
1–547（547 aa）
Chain J
1–547（547 aa）
Chain K
1–547（547 aa）
Chain L
1–547（547 aa）
Chain M
1–547（547 aa）
Chain N
1–547（547 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
12.5MM HEPES, 5MM KCL, 5MM MGCL2；pH 7.5；12.5MM HEPES, 5MM KCL, 5MM MGCL2
cryo-EM vitrification conditions
Cryogen ETHANE；LIQUID ETHANE
|
Resolution 8.70 Å |
| 2CGT GROEL-ADP-gp31 COMPLEX Deposited 2006-03-09 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric |
Chain A
1–547（547 aa）
Chain B
1–547（547 aa）
Chain C
1–547（547 aa）
Chain D
1–547（547 aa）
Chain E
1–547（547 aa）
Chain F
1–547（547 aa）
Chain G
1–547（547 aa）
Chain H
1–547（547 aa）
Chain I
1–547（547 aa）
Chain J
1–547（547 aa）
Chain K
1–547（547 aa）
Chain L
1–547（547 aa）
Chain M
1–547（547 aa）
Chain N
1–547（547 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
20MM TRIS-HCL, 10MM MGCL, 10MM KCL；pH 7.4；20MM TRIS-HCL, 10MM MGCL, 10MM KCL
cryo-EM vitrification conditions
Cryogen ETHANE；GRIDS WERE BLOTED FOR 2-3 SECONDS AND THEN LEFT TO EQUILIBRATE FOR 2-3 SECONDS AND THEN PLUNGED INTO LIQUID ETHANE
|
Resolution 8.20 Å |
| 2EU1 Crystal structure of the chaperonin GroEL-E461K Deposited 2005-10-28 | Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
|
Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8；277 K；Reservoir solution: 43% (v/v) MPD, 100mM Imidazole, 170mM MgCl2.6H2O, dissolved in the ratio 1:1.5 with 22.5mg/ml protein, 50mM TRIS-HCL, 10mM MgCl2, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 3.29 Å R-free 0.296 |
| 2EU1 Crystal structure of the chaperonin GroEL-E461K Deposited 2005-10-28 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric |
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8；277 K；Reservoir solution: 43% (v/v) MPD, 100mM Imidazole, 170mM MgCl2.6H2O, dissolved in the ratio 1:1.5 with 22.5mg/ml protein, 50mM TRIS-HCL, 10mM MgCl2, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 3.29 Å R-free 0.296 |
| 2EU1 Crystal structure of the chaperonin GroEL-E461K Deposited 2005-10-28 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 3 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric |
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8；277 K；Reservoir solution: 43% (v/v) MPD, 100mM Imidazole, 170mM MgCl2.6H2O, dissolved in the ratio 1:1.5 with 22.5mg/ml protein, 50mM TRIS-HCL, 10mM MgCl2, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 3.29 Å R-free 0.296 |
| 2EU1 Crystal structure of the chaperonin GroEL-E461K Deposited 2005-10-28 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 4 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
|
Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K Mutation：E461K | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8；277 K；Reservoir solution: 43% (v/v) MPD, 100mM Imidazole, 170mM MgCl2.6H2O, dissolved in the ratio 1:1.5 with 22.5mg/ml protein, 50mM TRIS-HCL, 10mM MgCl2, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K
|
Resolution 3.29 Å R-free 0.296 |
| 2YEY Crystal structure of the allosteric-defective chaperonin GroEL E434K mutant Deposited 2011-03-31 | Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
2–525（524 aa）
Chain B
2–525（524 aa）
Chain C
2–525（524 aa）
Chain D
2–525（524 aa）
Chain E
2–525（524 aa）
Chain F
2–525（524 aa）
Chain G
2–525（524 aa）
Chain H
2–525（524 aa）
Chain I
2–525（524 aa）
Chain J
2–525（524 aa）
Chain K
2–525（524 aa）
Chain L
2–525（524 aa）
Chain M
2–525（524 aa）
Chain N
2–525（524 aa）
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 4.50 Å R-free 0.240 |
| 3C9V C7 Symmetrized Structure of Unliganded GroEL at 4.7 Angstrom Resolution from CryoEM Deposited 2008-02-18 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
2–527（526 aa）
Fragment：residues 2-527
Chain B
2–527（526 aa）
Fragment：residues 2-527
Chain C
2–527（526 aa）
Fragment：residues 2-527
Chain D
2–527（526 aa）
Fragment：residues 2-527
Chain E
2–527（526 aa）
Fragment：residues 2-527
Chain F
2–527（526 aa）
Fragment：residues 2-527
Chain G
2–527（526 aa）
Fragment：residues 2-527
Chain H
2–527（526 aa）
Fragment：residues 2-527
Chain I
2–527（526 aa）
Fragment：residues 2-527
Chain J
2–527（526 aa）
Fragment：residues 2-527
Chain K
2–527（526 aa）
Fragment：residues 2-527
Chain L
2–527（526 aa）
Fragment：residues 2-527
Chain M
2–527（526 aa）
Fragment：residues 2-527
Chain N
2–527（526 aa）
Fragment：residues 2-527
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
20 mM Tris.HCl, pH 7.5, 50 mM MgCl2；pH 7.5；20 mM Tris.HCl, pH 7.5, 50 mM MgCl2
cryo-EM vitrification conditions
Cryogen ETHANE；ETHANE. Vitrobot, blot for 2 sec.
|
Resolution 4.70 Å |
| 3CAU D7 symmetrized structure of unliganded GroEL at 4.2 Angstrom resolution by cryoEM Deposited 2008-02-20 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
2–527（526 aa）
Fragment：residues 2-527
Chain B
2–527（526 aa）
Fragment：residues 2-527
Chain C
2–527（526 aa）
Fragment：residues 2-527
Chain D
2–527（526 aa）
Fragment：residues 2-527
Chain E
2–527（526 aa）
Fragment：residues 2-527
Chain F
2–527（526 aa）
Fragment：residues 2-527
Chain G
2–527（526 aa）
Fragment：residues 2-527
Chain H
2–527（526 aa）
Fragment：residues 2-527
Chain I
2–527（526 aa）
Fragment：residues 2-527
Chain J
2–527（526 aa）
Fragment：residues 2-527
Chain K
2–527（526 aa）
Fragment：residues 2-527
Chain L
2–527（526 aa）
Fragment：residues 2-527
Chain M
2–527（526 aa）
Fragment：residues 2-527
Chain N
2–527（526 aa）
Fragment：residues 2-527
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
20 mM Tris.HCl, pH 7.5, 50 mM MgCl2；pH 7.5；20 mM Tris.HCl, pH 7.5, 50 mM MgCl2
cryo-EM vitrification conditions
Cryogen ETHANE；ETHANE. Vitrobot, 2sec blot
|
Resolution 4.20 Å |
| 3VZ6 Crystal Structure Analysis of the Mini-chaperonines, variant with Gly 184 replaced with Ile and Leu 185 replaced Val and Val 186 replaced with Leu. Deposited 2012-10-09 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
191–376（186 aa）
Fragment：Apical domain, UNP residues 191-376
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.7；288 K；0.1M Tris-HCl,1M NaCl, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 288K
|
Resolution 1.50 Å R-free 0.288 |
| 3VZ7 Crystal Structure Analysis of the mini-chaperonin variant with Pro 187 Gly Deposited 2012-10-09 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
191–376（186 aa）
Fragment：Apical domain, UNP residues 191-376
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.7；288 K；0.1M Tris-HCl, 1M NaCl, 3.75% Glycerol, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 288K
|
Resolution 1.80 Å R-free 0.249 |
| 3VZ8 Crystal Structure Analysis of the Mini-chaperonin variant with Leu 185, Val 186, Pro 187, Arg 188 and Ser 190 replaced with all Gly Deposited 2012-10-09 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
191–376（186 aa）
Fragment：Apical domain, UNP residues 192-376
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.9；288 K；0.1M Tris-HCl, 1.61M NaCl, pH 7.9, VAPOR DIFFUSION, HANGING DROP, temperature 288K
|
Resolution 1.90 Å R-free 0.272 |
| 3VZ8 Crystal Structure Analysis of the Mini-chaperonin variant with Leu 185, Val 186, Pro 187, Arg 188 and Ser 190 replaced with all Gly Deposited 2012-10-09 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
191–376（186 aa）
Fragment：Apical domain, UNP residues 192-376
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.9；288 K；0.1M Tris-HCl, 1.61M NaCl, pH 7.9, VAPOR DIFFUSION, HANGING DROP, temperature 288K
|
Resolution 1.90 Å R-free 0.272 |
| 3VZ8 Crystal Structure Analysis of the Mini-chaperonin variant with Leu 185, Val 186, Pro 187, Arg 188 and Ser 190 replaced with all Gly Deposited 2012-10-09 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
191–376（186 aa）
Fragment：Apical domain, UNP residues 192-376
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.9；288 K；0.1M Tris-HCl, 1.61M NaCl, pH 7.9, VAPOR DIFFUSION, HANGING DROP, temperature 288K
|
Resolution 1.90 Å R-free 0.272 |
| 3WVL Crystal structure of the football-shaped GroEL-GroES complex (GroEL: GroES2:ATP14) from Escherichia coli Deposited 2014-05-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
|
Mutation：D52A, D398A Mutation：D52A, D398A Mutation：D52A, D398A Mutation：D52A, D398A Mutation：D52A, D398A Mutation：D52A, D398A Mutation：D52A, D398A | ATP ADENOSINE-5'-TRIPHOSPHATE × 7 MG MAGNESIUM ION × 7 K POTASSIUM ION × 7 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；35% PEG 550 MME, 0.1M HEPES, 1mM ATP, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 3.79 Å R-free 0.250 |
| 3WVL Crystal structure of the football-shaped GroEL-GroES complex (GroEL: GroES2:ATP14) from Escherichia coli Deposited 2014-05-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric |
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Mutation：D52A, D398A Mutation：D52A, D398A Mutation：D52A, D398A Mutation：D52A, D398A Mutation：D52A, D398A Mutation：D52A, D398A Mutation：D52A, D398A | ATP ADENOSINE-5'-TRIPHOSPHATE × 7 MG MAGNESIUM ION × 7 K POTASSIUM ION × 7 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；35% PEG 550 MME, 0.1M HEPES, 1mM ATP, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 3.79 Å R-free 0.250 |
| 3ZPZ Visualizing GroEL-ES in the Act of Encapsulating a Non-Native Substrate Protein Deposited 2013-03-04 | 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 × 21 PDB declaration: 21-meric |
Chain A
2–527（526 aa）
Chain B
2–527（526 aa）
Chain C
2–527（526 aa）
Chain D
2–527（526 aa）
Chain E
2–527（526 aa）
Chain F
2–527（526 aa）
Chain G
2–527（526 aa）
Chain H
2–527（526 aa）
Chain I
2–527（526 aa）
Chain J
2–527（526 aa）
Chain K
2–527（526 aa）
Chain L
2–527（526 aa）
Chain M
2–527（526 aa）
Chain N
2–527（526 aa）
|
Not recorded | MG MAGNESIUM ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 7 |
ELECTRON MICROSCOPY
cryo-EM buffer
50 MM HEPES, 5 MM KOAC, 10 MM MG(OAC)2, 2 MM DTT；pH 7.6；50 MM HEPES, 5 MM KOAC, 10 MM MG(OAC)2, 2 MM DTT
cryo-EM vitrification conditions
Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 95, TEMPERATURE- 98, INSTRUMENT- FEI VITROBOT MARK III, METHOD- BLOT FOR 1 SECOND BEFORE PLUNGING,
|
Resolution 8.90 Å |
| 3ZQ0 Visualizing GroEL-ES in the Act of Encapsulating a Non-Native Substrate Protein Deposited 2013-03-04 | 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 × 21 PDB declaration: 21-meric |
Chain A
2–525（524 aa）
Chain B
2–525（524 aa）
Chain C
2–525（524 aa）
Chain D
2–525（524 aa）
Chain E
2–525（524 aa）
Chain F
2–525（524 aa）
Chain G
2–525（524 aa）
Chain H
2–525（524 aa）
Chain I
2–525（524 aa）
Chain J
2–525（524 aa）
Chain K
2–525（524 aa）
Chain L
2–525（524 aa）
Chain M
2–525（524 aa）
Chain N
2–525（524 aa）
|
Not recorded | ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7 |
ELECTRON MICROSCOPY
cryo-EM buffer
50 MM HEPES, 50 MM KOAC, 10 MM MG(OAC)2, 2 MM DTT；pH 7.6；50 MM HEPES, 50 MM KOAC, 10 MM MG(OAC)2, 2 MM DTT
cryo-EM vitrification conditions
Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 95, TEMPERATURE- 98, INSTRUMENT- FEI VITROBOT MARK III, METHOD BLOT FOR 1 SECOND BEFORE PLUNGIN
|
Resolution 9.20 Å |
| 3ZQ1 Visualizing GroEL-ES in the Act of Encapsulating a Non-Native Substrate Protein Deposited 2013-03-04 | 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 × 21 PDB declaration: 21-meric |
Chain A
2–527（526 aa）
Chain B
2–527（526 aa）
Chain C
2–527（526 aa）
Chain D
2–527（526 aa）
Chain E
2–527（526 aa）
Chain F
2–527（526 aa）
Chain G
2–527（526 aa）
Chain H
2–527（526 aa）
Chain I
2–527（526 aa）
Chain J
2–527（526 aa）
Chain K
2–527（526 aa）
Chain L
2–527（526 aa）
Chain M
2–527（526 aa）
Chain N
2–527（526 aa）
|
Not recorded | MG MAGNESIUM ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 7 |
ELECTRON MICROSCOPY
cryo-EM buffer
50 MM HEPES, 50 MM KOAC, 10 MM MG(OAC)2, 2 MM DTT；pH 7.6；50 MM HEPES, 50 MM KOAC, 10 MM MG(OAC)2, 2 MM DTT
cryo-EM vitrification conditions
Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 95, TEMPERATURE- 98, INSTRUMENT- FEI VITROBOT MARK III, METHOD- BLOT FOR 1 SECOND BEFORE PLUNGING,
|
Resolution 15.90 Å |
| 4AAQ ATP-triggered molecular mechanics of the chaperonin GroEL Deposited 2011-12-05 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | ATP ADENOSINE-5'-TRIPHOSPHATE × 7 PO4 PHOSPHATE ION × 7 MG MAGNESIUM ION × 7 |
ELECTRON MICROSCOPY
cryo-EM buffer
50 MM TRIS-HCL PH 7.4, 50 MM KCL, 10 MM MGCL2 AND 200UM ATP；pH 7.4；50 MM TRIS-HCL PH 7.4, 50 MM KCL, 10 MM MGCL2 AND 200UM ATP
cryo-EM vitrification conditions
Cryogen ETHANE；VITRIFIED WITH A VITROBOT AT 100 PERCENT HUMIDITY WITH 2-3 SECONDS BLOTTING TIME
|
Resolution 8.00 Å |
| 4AAR ATP-triggered molecular mechanics of the chaperonin GroEL Deposited 2011-12-05 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | ATP ADENOSINE-5'-TRIPHOSPHATE × 7 PO4 PHOSPHATE ION × 7 MG MAGNESIUM ION × 7 |
ELECTRON MICROSCOPY
cryo-EM buffer
50 MM TRIS-HCL PH 7.4, 50 MM KCL AND 10 MM MGCL2, 200 UM ATP；pH 7.4；50 MM TRIS-HCL PH 7.4, 50 MM KCL AND 10 MM MGCL2, 200 UM ATP
cryo-EM vitrification conditions
Cryogen ETHANE；VITRIFIED WITH A VITROBOT AT 100 PERCENT HUMIDITY WITH 2-3 SECONDS BLOTTING TIME
|
Resolution 8.00 Å |
| 4AAS ATP-triggered molecular mechanics of the chaperonin GroEL Deposited 2011-12-05 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | PO4 PHOSPHATE ION × 7 MG MAGNESIUM ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 |
ELECTRON MICROSCOPY
cryo-EM buffer
50 MM TRIS-HCL PH 7.4, 50 MM KCL AND 10 MM MGCL2, 200 UM ATP；pH 7.4；50 MM TRIS-HCL PH 7.4, 50 MM KCL AND 10 MM MGCL2, 200 UM ATP
cryo-EM vitrification conditions
Cryogen ETHANE；VITRIFIED WITH A VITROBOT AT 100 PERCENT HUMIDITY WITH 2-3 SECONDS BLOTTING TIME
|
Resolution 8.50 Å |
| 4AAU ATP-triggered molecular mechanics of the chaperonin GroEL Deposited 2011-12-05 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | MG MAGNESIUM ION × 14 PO4 PHOSPHATE ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
50 MM TRIS-HCL PH 7.4, 50 MM KCL AND 10 MM MGCL2, 200 UM ATP；pH 7.4；50 MM TRIS-HCL PH 7.4, 50 MM KCL AND 10 MM MGCL2, 200 UM ATP
cryo-EM vitrification conditions
Cryogen ETHANE；VITRIFIED WITH A VITROBOT AT 100 PERCENT HUMIDITY WITH 2-3 SECONDS BLOTTING TIME
|
Resolution 8.50 Å |
| 4AB2 ATP-triggered molecular mechanics of the chaperonin GroEL Deposited 2011-12-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | ATP ADENOSINE-5'-TRIPHOSPHATE × 14 MG MAGNESIUM ION × 14 PO4 PHOSPHATE ION × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
50 MM TRIS-HCL PH 7.4, 50 MM KCL AND 10 MM MGCL2, 200 UM ATP；pH 7.4；50 MM TRIS-HCL PH 7.4, 50 MM KCL AND 10 MM MGCL2, 200 UM ATP
cryo-EM vitrification conditions
Cryogen ETHANE；VITRIFIED WITH A VITROBOT AT 100 PERCENT HUMIDITY WITH 2-3 SECONDS BLOTTING TIME
|
Resolution 8.50 Å |
| 4AB3 ATP-triggered molecular mechanics of the chaperonin GroEL Deposited 2011-12-06 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | PO4 PHOSPHATE ION × 14 MG MAGNESIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
50 MM TRIS-HCL PH 7.4, 50 MM KCL AND 10 MM MGCL2, 200 UM ATP；pH 7.4；50 MM TRIS-HCL PH 7.4, 50 MM KCL AND 10 MM MGCL2, 200 UM ATP
cryo-EM vitrification conditions
Cryogen ETHANE；VITRIFIED WITH A VITROBOT AT 100 PERCENT HUMIDITY WITH 2-3 SECONDS BLOTTING TIME
|
Resolution 8.50 Å |
| 4V43 Structural and mechanistic basis for allostery in the bacterial chaperonin GroEL Deposited 2002-01-02 | Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–547（547 aa）
Chain B
1–547（547 aa）
Chain C
1–547（547 aa）
Chain D
1–547（547 aa）
Chain E
1–547（547 aa）
Chain F
1–547（547 aa）
Chain G
1–547（547 aa）
Chain H
1–547（547 aa）
Chain I
1–547（547 aa）
Chain J
1–547（547 aa）
Chain K
1–547（547 aa）
Chain L
1–547（547 aa）
Chain M
1–547（547 aa）
Chain N
1–547（547 aa）
|
Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；pH 7.0
|
Resolution 3.52 Å R-free 0.298 |
| 4V43 Structural and mechanistic basis for allostery in the bacterial chaperonin GroEL Deposited 2002-01-02 | Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain 1
1–547（547 aa）
Chain 2
1–547（547 aa）
Chain O
1–547（547 aa）
Chain P
1–547（547 aa）
Chain Q
1–547（547 aa）
Chain R
1–547（547 aa）
Chain S
1–547（547 aa）
Chain T
1–547（547 aa）
Chain U
1–547（547 aa）
Chain V
1–547（547 aa）
Chain W
1–547（547 aa）
Chain X
1–547（547 aa）
Chain Y
1–547（547 aa）
Chain Z
1–547（547 aa）
|
Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A Mutation：D398A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；pH 7.0
|
Resolution 3.52 Å R-free 0.298 |
| 4WGL Crystal structure of a GroEL D83A/R197A double mutant Deposited 2014-09-19 | Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Mutation：D83A, R197A Mutation：D83A, R197A Mutation：D83A, R197A Mutation：D83A, R197A Mutation：D83A, R197A Mutation：D83A, R197A Mutation：D83A, R197A Mutation：D83A, R197A Mutation：D83A, R197A Mutation：D83A, R197A Mutation：D83A, R197A Mutation：D83A, R197A Mutation：D83A, R197A Mutation：D83A, R197A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；25% PEG 3000, 0.1M acetic acid
|
Resolution 3.13 Å R-free 0.233 |
| 5OPW Crystal structure of the GroEL mutant A109C Deposited 2017-08-10 | Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
2–548（547 aa）
Fragment：GroEL
Chain B
2–548（547 aa）
Fragment：GroEL
Chain C
2–548（547 aa）
Fragment：GroEL
Chain D
2–548（547 aa）
Fragment：GroEL
Chain E
2–548（547 aa）
Fragment：GroEL
Chain F
2–548（547 aa）
Fragment：GroEL
Chain G
2–548（547 aa）
Fragment：GroEL
Chain H
2–548（547 aa）
Fragment：GroEL
Chain I
2–548（547 aa）
Fragment：GroEL
Chain J
2–548（547 aa）
Fragment：GroEL
Chain K
2–548（547 aa）
Fragment：GroEL
Chain L
2–548（547 aa）
Fragment：GroEL
Chain M
2–548（547 aa）
Fragment：GroEL
Chain N
2–548（547 aa）
Fragment：GroEL
|
Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5.5；291 K；0.1 M sodium citrate, pH 5.5, and 15 % PEG 6000
|
Resolution 3.19 Å R-free 0.252 |
| 5OPX Crystal structure of the GroEL mutant A109C in complex with GroES and ADP BeF2 Deposited 2017-08-10 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 28 PDB declaration: 28-meric |
Chain A
1–548（548 aa）
Fragment：GroEL
Chain B
1–548（548 aa）
Fragment：GroEL
Chain C
1–548（548 aa）
Fragment：GroEL
Chain D
1–548（548 aa）
Fragment：GroEL
Chain E
1–548（548 aa）
Fragment：GroEL
Chain F
1–548（548 aa）
Fragment：GroEL
Chain G
1–548（548 aa）
Fragment：GroEL
Chain H
1–548（548 aa）
Fragment：GroEL
Chain I
1–548（548 aa）
Fragment：GroEL
Chain J
1–548（548 aa）
Fragment：GroEL
Chain K
1–548（548 aa）
Fragment：GroEL
Chain L
1–548（548 aa）
Fragment：GroEL
Chain M
1–548（548 aa）
Fragment：GroEL
Chain N
1–548（548 aa）
Fragment：GroEL
|
Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C Mutation：A109C | ADP ADENOSINE-5'-DIPHOSPHATE × 14 MG MAGNESIUM ION × 14 BEF BERYLLIUM TRIFLUORIDE ION × 14 K POTASSIUM ION × 14 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8；291 K；10 mM ATP, 3 mM BeF2, 0.1 M Tris, pH 8.0, 0.2 M NaCl and 20 % PEG 4000
|
Resolution 3.64 Å R-free 0.256 |
| 7PBJ Cryo-EM structure of the GroEL-GroES complex with ADP bound to both rings ("wide" conformation). Deposited 2021-08-02 | 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 × 21 PDB declaration: 21-meric |
Chain Ad
2–525（524 aa）
Chain Ae
2–525（524 aa）
Chain Ak
2–525（524 aa）
Chain Al
2–525（524 aa）
Chain Ar
2–525（524 aa）
Chain As
2–525（524 aa）
Chain Ay
2–525（524 aa）
Chain Az
2–525（524 aa）
Chain Bf
2–525（524 aa）
Chain Bg
2–525（524 aa）
Chain Bm
2–525（524 aa）
Chain Bn
2–525（524 aa）
Chain Bt
2–525（524 aa）
Chain Bu
2–525（524 aa）
|
Not recorded | ADP ADENOSINE-5'-DIPHOSPHATE × 14 MG MAGNESIUM ION × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.40 Å |
| 7PBX Cryo-EM structure of the GroEL-GroES complex with ADP bound to both rings ("tight" conformation). Deposited 2021-08-02 | 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 × 21 PDB declaration: 21-meric |
Chain Ac
2–525（524 aa）
Chain Ad
2–525（524 aa）
Chain Ai
2–525（524 aa）
Chain Aj
2–525（524 aa）
Chain Ao
2–525（524 aa）
Chain Ap
2–525（524 aa）
Chain Au
2–525（524 aa）
Chain Av
2–525（524 aa）
Chain Ba
2–525（524 aa）
Chain Bb
2–525（524 aa）
Chain Bg
2–525（524 aa）
Chain Bh
2–525（524 aa）
Chain Bm
2–525（524 aa）
Chain Bn
2–525（524 aa）
|
Not recorded | ADP ADENOSINE-5'-DIPHOSPHATE × 14 MG MAGNESIUM ION × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.43 Å |
| 7VWX CryoEM structure of football-shaped GroEL:ES2 with RuBisCO Deposited 2021-11-12 | Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 29 PDB declaration: 29-meric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 7.60 Å |
| 7XOJ Cryo-EM structure of GroEL bound to unfolded substrate (UGT1A) at 2.8 Ang. resolution (Consensus Refinement) Deposited 2022-05-01 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
2–548（547 aa）
Chain B
2–548（547 aa）
Chain C
2–548（547 aa）
Chain D
2–548（547 aa）
Chain E
2–548（547 aa）
Chain F
2–548（547 aa）
Chain G
2–548（547 aa）
Chain H
2–548（547 aa）
Chain I
2–548（547 aa）
Chain J
2–548（547 aa）
Chain K
2–548（547 aa）
Chain L
2–548（547 aa）
Chain M
2–548（547 aa）
Chain N
2–548（547 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5；Sample containing GorEL-UGT1A was made fresh and used without undergoing any freeze-thaw cycles to avoid degradation in the solution.
The sample was in a buffer solution of 150mM NaCl, 20mM Tris-HCl at pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE；3 ul of 33 mg/ml GroEL-UGT1A was placed on Holey carbon Quanitifoil copper grids (300 mesh size R1.2/1.3)
and blotted for 3 seconds (blot force =1)
|
Resolution 2.80 Å |
| 7XOK Cryo-EM structure of double occupied ring (DOR) of GroEL-UGT1A complex at 2.7 Ang. resolution Deposited 2022-05-01 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
2–548（547 aa）
Chain B
2–548（547 aa）
Chain C
2–548（547 aa）
Chain D
2–548（547 aa）
Chain E
2–548（547 aa）
Chain F
2–548（547 aa）
Chain G
2–548（547 aa）
Chain H
2–548（547 aa）
Chain I
2–548（547 aa）
Chain J
2–548（547 aa）
Chain K
2–548（547 aa）
Chain L
2–548（547 aa）
Chain M
2–548（547 aa）
Chain N
2–548（547 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5；Sample containing GorEL-UGT1A was made fresh and used without undergoing any freeze-thaw cycles to avoid degradation in the solution.
The sample was in a buffer solution of 150mM NaCl, 20mM Tris-HCl at pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE；3 ul of 33 mg/ml GroEL-UGT1A was placed on Holey carbon Quanitifoil copper grids (300 mesh size R1.2/1.3)
and blotted for 3 seconds (blot force =1)
|
Resolution 2.70 Å |
| 7XOL Cryo-EM structure of single empty ring 2 (SER2) of GroEL-UGT1A complex at 3.2 Ang. resolution Deposited 2022-05-01 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
2–548（547 aa）
Chain B
2–548（547 aa）
Chain C
2–548（547 aa）
Chain D
2–548（547 aa）
Chain E
2–548（547 aa）
Chain F
2–548（547 aa）
Chain G
2–548（547 aa）
Chain H
2–548（547 aa）
Chain I
2–548（547 aa）
Chain J
2–548（547 aa）
Chain K
2–548（547 aa）
Chain L
2–548（547 aa）
Chain M
2–548（547 aa）
Chain N
2–548（547 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5；Sample containing GorEL-UGT1A was made fresh and used without undergoing any freeze-thaw cycles to avoid degradation in the solution.
The sample was in a buffer solution of 150mM NaCl, 20mM Tris-HCl at pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE；3 ul of 33 mg/ml GroEL-UGT1A was placed on Holey carbon Quanitifoil copper grids (300 mesh size R1.2/1.3)
and blotted for 3 seconds (blot force =1)
|
Resolution 3.26 Å |
| 7XOM Cryo-EM structure of occupied ring subunit 4 (OR4) of GroEL complexed with polyalanine model of UGT1A from GroEL-UGT1A double occupied ring complex Deposited 2022-05-01 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric |
Chain A
2–548（547 aa）
Chain B
2–548（547 aa）
Chain C
2–548（547 aa）
Chain D
2–548（547 aa）
Chain E
2–548（547 aa）
Chain F
2–548（547 aa）
Chain G
2–548（547 aa）
Chain H
2–548（547 aa）
Chain I
2–548（547 aa）
Chain J
2–548（547 aa）
Chain K
2–548（547 aa）
Chain L
2–548（547 aa）
Chain M
2–548（547 aa）
Chain N
2–548（547 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5；Sample containing GorEL-UGT1A was made fresh and used without undergoing any freeze-thaw cycles to avoid degradation in the solution.
The sample was in a buffer solution of 150mM NaCl, 20mM Tris-HCl at pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE；3 ul of 33 mg/ml GroEL-UGT1A was placed on Holey carbon Quanitifoil copper grids (300 mesh size R1.2/1.3)
and blotted for 3 seconds (blot force =1)
|
Resolution 3.20 Å |
| 7XON Cryo-EM structure of empty ring subunit 1 (ER1) from single empty ring of GroEL-UGT1A complex Deposited 2022-05-01 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–548（547 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5；Sample containing GorEL-UGT1A was made fresh and used without undergoing any freeze-thaw cycles to avoid degradation in the solution.
The sample was in a buffer solution of 150mM NaCl, 20mM Tris-HCl at pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE；3 ul of 33 mg/ml GroEL-UGT1A was placed on Holey carbon Quanitifoil copper grids (300 mesh size R1.2/1.3)
and blotted for 3 seconds (blot force =1)
|
Resolution 3.10 Å |
| 7XOO Cryo-EM structure of empty ring subunit 2 (ER2) from GroEL-UGT1A single empty ring complex Deposited 2022-05-01 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–548（547 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5；Sample containing GorEL-UGT1A was made fresh and used without undergoing any freeze-thaw cycles to avoid degradation in the solution.
The sample was in a buffer solution of 150mM NaCl, 20mM Tris-HCl at pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE；3 ul of 33 mg/ml GroEL-UGT1A was placed on Holey carbon Quanitifoil copper grids (300 mesh size R1.2/1.3)
and blotted for 3 seconds (blot force =1)
|
Resolution 3.00 Å |
| 7XOP Cryo-EM structure of occupied ring subunit 1 (OR1) of GroEL from GroEL-UGT1A double occupied ring complex Deposited 2022-05-01 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain K
2–548（547 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5；Sample containing GorEL-UGT1A was made fresh and used without undergoing any freeze-thaw cycles to avoid degradation in the solution.
The sample was in a buffer solution of 150mM NaCl, 20mM Tris-HCl, 150mM NaCl at pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE；3 ul of 33 mg/ml GroEL-UGT1A was placed on Holey carbon Quanitifoil copper grids (300 mesh size R1.2/1.3)
and blotted for 3 seconds (blot force =1)
|
Resolution 3.20 Å |
| 7XOQ Cryo-EM structure of occupied ring subunit 2 (OR2) of GroEL from GroEL-UGT1A double occupied ring complex Deposited 2022-05-01 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain K
2–548（547 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5；Sample containing GorEL-UGT1A was made fresh and used without undergoing any freeze-thaw cycles to avoid degradation in the solution.
The sample was in a buffer solution of 150mM NaCl, 20mM Tris-HCl at pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE；3 ul of 33 mg/ml GroEL-UGT1A was placed on Holey carbon Quanitifoil copper grids (300 mesh size R1.2/1.3)
and blotted for 3 seconds (blot force =1)
|
Resolution 3.30 Å |
| 7XOR Cryo-EM structure of occupied ring subunit 3 (OR3) of GroEL from GroEL-UGT1A double occupied ring complex Deposited 2022-05-01 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain K
2–548（547 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5；Sample containing GorEL-UGT1A was made fresh and used without undergoing any freeze-thaw cycles to avoid degradation in the solution.
The sample was in a buffer solution of 150mM NaCl, 20mM Tris-HCl at pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE；3 ul of 33 mg/ml GroEL-UGT1A was placed on Holey carbon Quanitifoil copper grids (300 mesh size R1.2/1.3)
and blotted for 3 seconds (blot force =1)
|
Resolution 3.30 Å |
| 7XOS Cryo-EM structure of occupied ring subunit 4 (OR4) of GroEL from GroEL-UGT1A double occupied ring complex Deposited 2022-05-01 | Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain K
2–548（547 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5；Sample containing GorEL-UGT1A was made fresh and used without undergoing any freeze-thaw cycles to avoid degradation in the solution.
The sample was in a buffer solution of 150mM NaCl, 20mM Tris-HCl at pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE；3 ul of 33 mg/ml GroEL-UGT1A was placed on Holey carbon Quanitifoil copper grids (300 mesh size R1.2/1.3)
and blotted for 3 seconds (blot force =1)
|
Resolution 3.20 Å |
| 8BA7 CryoEM structure of nucleotide-free GroEL-Rubisco. Deposited 2022-10-11 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
2–548（547 aa）
Chain B
2–548（547 aa）
Chain C
2–548（547 aa）
Chain D
2–548（547 aa）
Chain E
2–548（547 aa）
Chain F
2–548（547 aa）
Chain G
2–548（547 aa）
Chain H
2–548（547 aa）
Chain I
2–548（547 aa）
Chain J
2–548（547 aa）
Chain K
2–548（547 aa）
Chain L
2–548（547 aa）
Chain M
2–548（547 aa）
Chain N
2–548（547 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE；The grid was prepared using a chameleon (SPT Labtech).
|
Resolution 4.40 Å |
| 8BA8 CryoEM structure of GroEL-ADP.BeF3-Rubisco. Deposited 2022-10-11 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: 14-meric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Not recorded | BEF BERYLLIUM TRIFLUORIDE ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 14 MG MAGNESIUM ION × 14 K POTASSIUM ION × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE；The grid was prepared using a chameleon (SPT Labtech).
|
Resolution 3.40 Å |
| 8BA9 CryoEM structure of GroEL-GroES-ADP.AlF3-Rubisco. Deposited 2022-10-11 | 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 × 21 PDB declaration: 21-meric |
Chain A
2–525（524 aa）
Chain B
2–525（524 aa）
Chain C
2–525（524 aa）
Chain D
2–525（524 aa）
Chain E
2–525（524 aa）
Chain F
2–525（524 aa）
Chain G
2–525（524 aa）
Chain H
2–525（524 aa）
Chain I
2–525（524 aa）
Chain J
2–525（524 aa）
Chain K
2–525（524 aa）
Chain L
2–525（524 aa）
Chain M
2–525（524 aa）
Chain N
2–525（524 aa）
|
Not recorded | AF3 ALUMINUM FLUORIDE × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 14 MG MAGNESIUM ION × 14 K POTASSIUM ION × 7 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE；The grid was prepared using a chameleon (SPT Labtech).
|
Resolution 3.70 Å |
| 8BAA CryoEM structure of GroEL-GroES-ADP.AlF3-Rubisco, class II. Deposited 2022-10-11 | 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 × 22 PDB declaration: 22-meric |
Chain A
2–548（547 aa）
Chain B
2–548（547 aa）
Chain C
2–548（547 aa）
Chain D
2–548（547 aa）
Chain E
2–548（547 aa）
Chain F
2–548（547 aa）
Chain G
2–548（547 aa）
Chain H
2–548（547 aa）
Chain I
2–548（547 aa）
Chain J
2–548（547 aa）
Chain K
2–548（547 aa）
Chain L
2–548（547 aa）
Chain M
2–548（547 aa）
Chain N
2–548（547 aa）
|
Not recorded | AF3 ALUMINUM FLUORIDE × 7 MG MAGNESIUM ION × 14 ADP ADENOSINE-5'-DIPHOSPHATE × 14 K POTASSIUM ION × 7 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE；The grid was prepared using a chameleon (SPT Labtech).
|
Resolution 4.20 Å |
| 8BKZ GroEL:GroES-ATP complex under continuous turnover conditions Deposited 2022-11-09 | 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 × 28 PDB declaration: 28-meric |
Chain A
1–548（548 aa）
Chain BA
1–548（548 aa）
Chain C
1–548（548 aa）
Chain E
1–548（548 aa）
Chain G
1–548（548 aa）
Chain I
1–548（548 aa）
Chain K
1–548（548 aa）
Chain M
1–548（548 aa）
Chain O
1–548（548 aa）
Chain Q
1–548（548 aa）
Chain S
1–548（548 aa）
Chain V
1–548（548 aa）
Chain X
1–548（548 aa）
Chain Z
1–548（548 aa）
|
Not recorded | MG MAGNESIUM ION × 14 K POTASSIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.30 Å |
| 8BL2 Structure of GroEL-ATP complex plunge frozen 200 ms after reaction initiation Deposited 2022-11-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Not recorded | MG MAGNESIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 14 K POTASSIUM ION × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.30 Å |
| 8BL7 Structure of GroEL-nucleotide complex in ADP-like conformation plunged 13 ms after mixing with ATP Deposited 2022-11-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.40 Å |
| 8BLC Structure of the GroEL-ATP complex plunge-frozen 50 ms after mixing with ATP Deposited 2022-11-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Not recorded | MG MAGNESIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 14 K POTASSIUM ION × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.70 Å |
| 8BLD Structure of the GroEL(ATP7/ADP7) complex plunged 13 ms after mixing with ATP Deposited 2022-11-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.40 Å |
| 8BLE Structure of GroEL-nucleotide complex in ADP-like conformation plunged 50 ms after mixing with ATP Deposited 2022-11-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.00 Å |
| 8BLF Structure of the GroEL(ATP7/ADP7) complex plunged 50 ms after mixing with ATP Deposited 2022-11-09 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.90 Å |
| 8BLY Structure of the GroEL-ATP complex plunge-frozen 13 ms after mixing with ATP Deposited 2022-11-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Not recorded | MG MAGNESIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.20 Å |
| 8BM0 Structure of GroEL:GroES-ATP complex plunge frozen 200 ms after reaction initiation Deposited 2022-11-10 | 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 × 21 PDB declaration: 21-meric |
Chain A
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain N
1–548（548 aa）
Chain O
1–548（548 aa）
Chain Q
1–548（548 aa）
Chain R
1–548（548 aa）
Chain T
1–548（548 aa）
|
Not recorded | MG MAGNESIUM ION × 14 K POTASSIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.40 Å |
| 8BM1 Structure of GroEL:GroES-ATP complex under continuous turnover conditions Deposited 2022-11-10 | 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 × 21 PDB declaration: 21-meric |
Chain A
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain N
1–548（548 aa）
Chain O
1–548（548 aa）
Chain Q
1–548（548 aa）
Chain R
1–548（548 aa）
Chain T
1–548（548 aa）
|
Not recorded | MG MAGNESIUM ION × 14 K POTASSIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.70 Å |
| 8BMD Structure of GroEL-ATP complex under continuous turnover conditions Deposited 2022-11-10 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Not recorded | MG MAGNESIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 14 K POTASSIUM ION × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.80 Å |
| 8BMO Structure of GroEL:GroES complex exhibiting ADP-conformation in trans ring obtained under the continuous turnover conditions Deposited 2022-11-10 | 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 × 21 PDB declaration: 21-meric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain O
1–548（548 aa）
Chain P
1–548（548 aa）
Chain R
1–548（548 aa）
Chain S
1–548（548 aa）
|
Not recorded | MG MAGNESIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.40 Å |
| 8BMT Structure of GroEL:GroES-ATP complex plunge frozen 200 ms after reaction initiation Deposited 2022-11-10 | 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 × 28 PDB declaration: 28-meric |
Chain A
1–548（548 aa）
Chain BA
1–548（548 aa）
Chain C
1–548（548 aa）
Chain E
1–548（548 aa）
Chain G
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain L
1–548（548 aa）
Chain N
1–548（548 aa）
Chain P
1–548（548 aa）
Chain R
1–548（548 aa）
Chain T
1–548（548 aa）
Chain X
1–548（548 aa）
Chain Z
1–548（548 aa）
|
Not recorded | MG MAGNESIUM ION × 14 K POTASSIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.50 Å |
| 8P4M CryoEM structure of a C7-symmetrical GroEL7-GroES7 cage in presence of ADP-BeFx Deposited 2023-05-23 | 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 × 14 PDB declaration: tetradecameric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
|
Not recorded | ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7 BEF BERYLLIUM TRIFLUORIDE ION × 7 K POTASSIUM ION × 7 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE-PROPANE；5.9 mM n-octyl-beta-D-glucopyranoside were added before vitrification
|
Resolution 2.50 Å |
| 8P4N CryoEM structure of a GroEL7-GroES7 cage with encapsulated disordered substrate MetK in the presence of ADP-BeFx Deposited 2023-05-23 | 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 × 14 PDB declaration: tetradecameric |
Chain A
2–548（547 aa）
Chain B
2–548（547 aa）
Chain C
2–548（547 aa）
Chain D
2–548（547 aa）
Chain E
2–548（547 aa）
Chain F
2–548（547 aa）
Chain G
2–548（547 aa）
|
Not recorded | ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7 BEF BERYLLIUM TRIFLUORIDE ION × 7 K POTASSIUM ION × 7 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE-PROPANE；5.9 mM n-octyl-beta-D-glucopyranoside were added before vitrification
|
Resolution 2.90 Å |
| 8P4O CryoEM structure of a GroEL7-GroES7 cage with encapsulated ordered substrate MetK in the presence of ADP-BeFx Deposited 2023-05-23 | 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 × 15 PDB declaration: pentadecameric |
Chain A
2–548（547 aa）
Chain B
2–548（547 aa）
Chain C
2–548（547 aa）
Chain D
2–548（547 aa）
Chain E
2–548（547 aa）
Chain F
2–548（547 aa）
Chain G
2–548（547 aa）
|
Not recorded | ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7 BEF BERYLLIUM TRIFLUORIDE ION × 7 K POTASSIUM ION × 7 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE-PROPANE；5.9 mM n-octyl-beta-D-glucopyranoside were added before vitrification
|
Resolution 3.04 Å |
| 8QXS CryoEM structure of a GroEL14-GroES7 complex in presence of ADP-BeFx with wide GroEL7 trans ring conformation Deposited 2023-10-25 | 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 × 21 PDB declaration: 21-meric |
Chain A
2–548（547 aa）
Chain B
2–548（547 aa）
Chain C
2–548（547 aa）
Chain D
2–548（547 aa）
Chain E
2–548（547 aa）
Chain F
2–548（547 aa）
Chain G
2–548（547 aa）
Chain H
2–548（547 aa）
Chain I
2–548（547 aa）
Chain J
2–548（547 aa）
Chain K
2–548（547 aa）
Chain L
2–548（547 aa）
Chain M
2–548（547 aa）
Chain N
2–548（547 aa）
|
Not recorded | ADP ADENOSINE-5'-DIPHOSPHATE × 14 MG MAGNESIUM ION × 14 BEF BERYLLIUM TRIFLUORIDE ION × 7 K POTASSIUM ION × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE-PROPANE；5.9 mM n-octyl-beta-D-glucopyranoside were added before vitrification
|
Resolution 3.12 Å |
| 8QXT CryoEM structure of a GroEL14-GroES7 complex in presence of ADP-BeFx with narrow GroEL7 trans ring conformation Deposited 2023-10-25 | 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 × 21 PDB declaration: 21-meric |
Chain A
2–548（547 aa）
Chain B
2–548（547 aa）
Chain C
2–548（547 aa）
Chain D
2–548（547 aa）
Chain E
2–548（547 aa）
Chain F
2–548（547 aa）
Chain G
2–548（547 aa）
Chain H
2–548（547 aa）
Chain I
2–548（547 aa）
Chain J
2–548（547 aa）
Chain K
2–548（547 aa）
Chain L
2–548（547 aa）
Chain M
2–548（547 aa）
Chain N
2–548（547 aa）
|
Not recorded | ADP ADENOSINE-5'-DIPHOSPHATE × 14 MG MAGNESIUM ION × 14 BEF BERYLLIUM TRIFLUORIDE ION × 7 K POTASSIUM ION × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE-PROPANE；5.9 mM n-octyl-beta-D-glucopyranoside were added before vitrification
|
Resolution 2.90 Å |
| 8QXU In situ structure average of GroEL14-GroES7 complexes with wide GroEL7 trans ring conformation in Escherichia coli cytosol obtained by cryo electron tomography Deposited 2023-10-25 | 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 × 21 PDB declaration: 21-meric |
Chain A
2–548（547 aa）
Chain B
2–548（547 aa）
Chain C
2–548（547 aa）
Chain D
2–548（547 aa）
Chain E
2–548（547 aa）
Chain F
2–548（547 aa）
Chain G
2–548（547 aa）
Chain H
2–548（547 aa）
Chain I
2–548（547 aa）
Chain J
2–548（547 aa）
Chain K
2–548（547 aa）
Chain L
2–548（547 aa）
Chain M
2–548（547 aa）
Chain N
2–548（547 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 7 MG MAGNESIUM ION × 14 K POTASSIUM ION × 14 ADP ADENOSINE-5'-DIPHOSPHATE × 7 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE-PROPANE
|
Resolution 12.00 Å |
| 8QXV In situ structure average of GroEL14-GroES7 complexes with narrow GroEL7 trans ring conformation in Escherichia coli cytosol obtained by cryo electron tomography Deposited 2023-10-25 | 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 × 21 PDB declaration: 21-meric |
Chain A
2–548（547 aa）
Chain B
2–548（547 aa）
Chain C
2–548（547 aa）
Chain D
2–548（547 aa）
Chain E
2–548（547 aa）
Chain F
2–548（547 aa）
Chain G
2–548（547 aa）
Chain H
2–548（547 aa）
Chain I
2–548（547 aa）
Chain J
2–548（547 aa）
Chain K
2–548（547 aa）
Chain L
2–548（547 aa）
Chain M
2–548（547 aa）
Chain N
2–548（547 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 7 MG MAGNESIUM ION × 14 K POTASSIUM ION × 14 ADP ADENOSINE-5'-DIPHOSPHATE × 7 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE-PROPANE
|
Resolution 13.60 Å |
| 8S32 GroEL with bound GroTAC peptide Deposited 2024-02-19 | Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 28 PDB declaration: 28-meric |
Chain A
1–548（548 aa）
Chain B
1–548（548 aa）
Chain C
1–548（548 aa）
Chain D
1–548（548 aa）
Chain E
1–548（548 aa）
Chain F
1–548（548 aa）
Chain G
1–548（548 aa）
Chain H
1–548（548 aa）
Chain I
1–548（548 aa）
Chain J
1–548（548 aa）
Chain K
1–548（548 aa）
Chain L
1–548（548 aa）
Chain M
1–548（548 aa）
Chain N
1–548（548 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8；ATP was added to the sample immediately before disposing on a grid
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.45 Å |
| 9YKC Cryo-EM structure of GroEL-gammaATP Deposited 2025-10-06 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
2–526（525 aa）
Chain B
2–526（525 aa）
Chain C
2–526（525 aa）
Chain D
2–526（525 aa）
Chain E
2–526（525 aa）
Chain F
2–526（525 aa）
Chain G
2–526（525 aa）
Chain H
2–526（525 aa）
Chain I
2–526（525 aa）
Chain J
2–526（525 aa）
Chain K
2–526（525 aa）
Chain L
2–526（525 aa）
Chain M
2–526（525 aa）
Chain N
2–526（525 aa）
|
Not recorded | AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.30 Å |
| 9YKE GroEL Apoenzyme Deposited 2025-10-07 | Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric |
Chain A
2–526（525 aa）
Chain B
2–526（525 aa）
Chain C
2–526（525 aa）
Chain D
2–526（525 aa）
Chain E
2–526（525 aa）
Chain F
2–526（525 aa）
Chain G
2–526（525 aa）
Chain H
2–526（525 aa）
Chain I
2–526（525 aa）
Chain J
2–526（525 aa）
Chain K
2–526（525 aa）
Chain L
2–526（525 aa）
Chain M
2–526（525 aa）
Chain N
2–526（525 aa）
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.70 Å |
| 9YNJ Cryo-EM structure of GroEL-ADP Deposited 2025-10-10 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: 14-meric |
Chain A
2–526（525 aa）
Chain B
2–526（525 aa）
Chain C
2–526（525 aa）
Chain D
2–526（525 aa）
Chain E
2–526（525 aa）
Chain F
2–526（525 aa）
Chain G
2–526（525 aa）
Chain H
2–526（525 aa）
Chain I
2–526（525 aa）
Chain J
2–526（525 aa）
Chain K
2–526（525 aa）
Chain L
2–526（525 aa）
Chain M
2–526（525 aa）
Chain N
2–526（525 aa）
|
Not recorded | ADP ADENOSINE-5'-DIPHOSPHATE × 14 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.20 Å |
81 other PDB entries and 95 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | CH60_ECOLI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–548； UniProt 1–548 Author chain B； PDBConstruct 1–548； UniProt 1–548 Author chain C； PDBConstruct 1–548； UniProt 1–548 Author chain D； PDBConstruct 1–548； UniProt 1–548 Author chain E； PDBConstruct 1–548； UniProt 1–548 Author chain F； PDBConstruct 1–548； UniProt 1–548 Author chain G； PDBConstruct 1–548； UniProt 1–548 Author chain H； PDBConstruct 1–548； UniProt 1–548 Author chain I； PDBConstruct 1–548； UniProt 1–548 Author chain J； PDBConstruct 1–548； UniProt 1–548 Author chain K； PDBConstruct 1–548； UniProt 1–548 Author chain L； PDBConstruct 1–548； UniProt 1–548 Author chain M； PDBConstruct 1–548； UniProt 1–548 Author chain N； PDBConstruct 1–548； UniProt 1–548 |
