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Protein Structures and Oligomeric States

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

Current Protein Identity：P06621 New Search
3PDB entries
7Biological assembly
20chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state 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
1CG2 CARBOXYPEPTIDASE G2 Deposited 1996-12-20 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 23–415（393 aa）
Chain B 23–415（393 aa）
Chain C 23–415（393 aa）
Chain D 23–415（393 aa）
Not recorded ZN ZINC ION × 13 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；291 K；HANGING DROPS WERE FORMED BY MIXING 4 MICROLITERS OF PROTEIN SOLUTION AT 16-20 MG/ML WITH 4 MICROLITERS OF RESERVOIR SOLUTION CONTAINING 10-12% PEG 4000, 0.2M TRIS (PH 7.2), 0.2M ZINC ACETATE 10% GLYCEROL. CRYSTALS GREW AT 18-20 DEGREES WITHIN A FEW DAYS., vapor diffusion - hanging drop, temperature 291K
Resolution 2.50 Å R-free 0.224
6XJ5 Carboxypeptidase G2 modified with a versatile bioconjugate for metalloprotein design Deposited 2020-06-22 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 24–415（392 aa）
Chain B 24–415（392 aa）
Mutation：S203C Mutation：S203C Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；Reservoir consisted of 750 uL of 0.2 M Tris pH 7.5, 10% PEG 3350, and 5% glycerol. 2 uL of reservoir solution was mixed with 2 uL of protein solution, consisting of 4.7 mg/mL CPG2 in 50 mM Tris 100 mM NaCl pH 7.4 supplemented with 0.1 M ZnSO4
Resolution 3.11 Å R-free 0.309
6XJ5 Carboxypeptidase G2 modified with a versatile bioconjugate for metalloprotein design Deposited 2020-06-22 Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 24–415（392 aa）
Chain D 24–415（392 aa）
Mutation：S203C Mutation：S203C Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 14 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；Reservoir consisted of 750 uL of 0.2 M Tris pH 7.5, 10% PEG 3350, and 5% glycerol. 2 uL of reservoir solution was mixed with 2 uL of protein solution, consisting of 4.7 mg/mL CPG2 in 50 mM Tris 100 mM NaCl pH 7.4 supplemented with 0.1 M ZnSO4
Resolution 3.11 Å R-free 0.309
6XJ5 Carboxypeptidase G2 modified with a versatile bioconjugate for metalloprotein design Deposited 2020-06-22 Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain E 24–415（392 aa）
Chain F 24–415（392 aa）
Mutation：S203C Mutation：S203C Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 17 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；Reservoir consisted of 750 uL of 0.2 M Tris pH 7.5, 10% PEG 3350, and 5% glycerol. 2 uL of reservoir solution was mixed with 2 uL of protein solution, consisting of 4.7 mg/mL CPG2 in 50 mM Tris 100 mM NaCl pH 7.4 supplemented with 0.1 M ZnSO4
Resolution 3.11 Å R-free 0.309
6XJ5 Carboxypeptidase G2 modified with a versatile bioconjugate for metalloprotein design Deposited 2020-06-22 Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain G 24–415（392 aa）
Chain H 24–415（392 aa）
Mutation：S203C Mutation：S203C Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 13 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；Reservoir consisted of 750 uL of 0.2 M Tris pH 7.5, 10% PEG 3350, and 5% glycerol. 2 uL of reservoir solution was mixed with 2 uL of protein solution, consisting of 4.7 mg/mL CPG2 in 50 mM Tris 100 mM NaCl pH 7.4 supplemented with 0.1 M ZnSO4
Resolution 3.11 Å R-free 0.309
7M6U Crystal structure of a circular permutation and computationally designed pro-enzyme of carboxypeptidase G2 Deposited 2021-03-26 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 89–415（327 aa）
Chain A 25–88（64 aa）
Chain C 89–415（327 aa）
Chain C 25–88（64 aa）
Mutation：K177A Mutation：K177A Mutation：K177A Mutation：K177A ZN ZINC ION × 11 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；Protein was prepared to a concentration of 19 mg/mL in 50 mM Tris 100 mM NaCl pH 7.4 0.2 mM ZnSO4. Reservoirs containing 750 uL of 20 mM Tris pH 8.0, 10% glycerol, and 10% PEG 3350 were prepared in 24 well hanging drop vapor diffusion plates. Equal volumes of protein solution and reservoir solution were mixed on a cover slip and suspended over the reservoir
Resolution 2.59 Å R-free 0.279
7M6U Crystal structure of a circular permutation and computationally designed pro-enzyme of carboxypeptidase G2 Deposited 2021-03-26 Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 89–415（327 aa）
Chain B 25–88（64 aa）
Chain D 89–415（327 aa）
Chain D 25–88（64 aa）
Mutation：K177A Mutation：K177A Mutation：K177A Mutation：K177A ZN ZINC ION × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；Protein was prepared to a concentration of 19 mg/mL in 50 mM Tris 100 mM NaCl pH 7.4 0.2 mM ZnSO4. Reservoirs containing 750 uL of 20 mM Tris pH 8.0, 10% glycerol, and 10% PEG 3350 were prepared in 24 well hanging drop vapor diffusion plates. Equal volumes of protein solution and reservoir solution were mixed on a cover slip and suspended over the reservoir
Resolution 2.59 Å R-free 0.279

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