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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：V9P0A9 New Search
5PDB entries
9Biological assembly
54chain/assembly records
Main Difference Dimensions in This Set
Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics

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

Related-Structure Differences

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

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
4D06 Bacterial chalcone isomerase complexed with naringenin Deposited 2014-04-24 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–283（283 aa）
Chain B 1–283（283 aa）
Chain C 1–283（283 aa）
Chain D 1–283（283 aa）
Chain E 1–283（283 aa）
Chain F 1–283（283 aa）
Not recorded NAR NARINGENIN × 7 CL CHLORIDE ION × 17 X8W (2E)-3-(4-hydroxyphenyl)-1-(2,4,6-trihydroxyphenyl)prop-2-en-1-one × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；0.1 M HEPES PH 7.5, 0.2 M SODIUM CHLORIDE, 1.6 M AMMONIUM SULFATE, 380 MIKROM NARINGENIN CHALCONE DISSOLVED IN ETHANOL
Resolution 2.00 Å R-free 0.163
4D4F Mutant P250A of bacterial chalcone isomerase from Eubacterium ramulus Deposited 2014-10-28 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–283（283 aa）
Chain B 1–283（283 aa）
Chain C 1–283（283 aa）
Chain D 1–283（283 aa）
Chain E 1–283（283 aa）
Chain F 1–283（283 aa）
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES GOL GLYCEROL × 11 CL CHLORIDE ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；2.0 M AMMONIUM SULPHATE, 0.1 M HEPES PH 7.5, 0.2 SODIUM CHLORIDE; CRYO: 2.4 M AMMONIUM SULPHATE, 22% GLYCEROL, 0.1 M HEPES PH 7.5, 0.2 SODIUM CHLORIDE
Resolution 2.34 Å R-free 0.175
8B7R Bacterial chalcone isomerase with taxifolin chalcone Deposited 2022-10-02 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–283（283 aa）
Chain B 1–283（283 aa）
Chain C 1–283（283 aa）
Chain D 1–283（283 aa）
Chain E 1–283（283 aa）
Chain F 1–283（283 aa）
Not recorded Q0X (Z)-3-[3,4-bis(oxidanyl)phenyl]-2-oxidanyl-1-[2,4,6-tris(oxidanyl)phenyl]prop-2-en-1-one × 6 CL CHLORIDE ION × 26 K POTASSIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；6.8 mg/ml CHI 50 mM Na phosphate, pH 6.8. Precipitant 1.8 M (NH4)2SO4, 0.2 M NaCl, 0.1 M HEPES pH 7.5. Soaking for 10 min in 2.5 mM taxifolin (2.5% ethanol)
Resolution 2.15 Å R-free 0.190
8B7U Bacterial chalcone isomerase H33A with taxifolin Deposited 2022-10-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–283（283 aa）
Chain B 1–283（283 aa）
Chain K 1–283（283 aa）
Chain L 1–283（283 aa）
Chain M 1–283（283 aa）
Chain N 1–283（283 aa）
Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A DQH (2R,3R)-2-(3,4-DIHYDROXYPHENYL)-3,5,7-TRIHYDROXY-2,3-DIHYDRO-4H-CHROMEN-4-ONE × 12 CL CHLORIDE ION × 18 GOL GLYCEROL × 1 SO4 SULFATE ION × 2 K POTASSIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；6.8 mg/ml CHI 50 mM Na phosphate, pH 6.8. Precipitant 1.5 M (NH4)2SO4, 0.2 M NaCl, 0.1 M HEPES pH 7.5. Hanging drop 2+2 ul. soaking for 10 min in 2.5 mM taxifolin (2.5% ethanol)
Resolution 2.80 Å R-free 0.225
8B7U Bacterial chalcone isomerase H33A with taxifolin Deposited 2022-10-03 Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain C 1–283（283 aa）
Chain D 1–283（283 aa）
Chain E 1–283（283 aa）
Chain F 1–283（283 aa）
Chain G 1–283（283 aa）
Chain H 1–283（283 aa）
Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A DQH (2R,3R)-2-(3,4-DIHYDROXYPHENYL)-3,5,7-TRIHYDROXY-2,3-DIHYDRO-4H-CHROMEN-4-ONE × 12 CL CHLORIDE ION × 16 GOL GLYCEROL × 1 SO4 SULFATE ION × 4 K POTASSIUM ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；6.8 mg/ml CHI 50 mM Na phosphate, pH 6.8. Precipitant 1.5 M (NH4)2SO4, 0.2 M NaCl, 0.1 M HEPES pH 7.5. Hanging drop 2+2 ul. soaking for 10 min in 2.5 mM taxifolin (2.5% ethanol)
Resolution 2.80 Å R-free 0.225
8B7U Bacterial chalcone isomerase H33A with taxifolin Deposited 2022-10-03 Assembly 3 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain I 1–283（283 aa）
Chain J 1–283（283 aa）
Chain O 1–283（283 aa）
Chain P 1–283（283 aa）
Chain Q 1–283（283 aa）
Chain R 1–283（283 aa）
Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A DQH (2R,3R)-2-(3,4-DIHYDROXYPHENYL)-3,5,7-TRIHYDROXY-2,3-DIHYDRO-4H-CHROMEN-4-ONE × 11 CL CHLORIDE ION × 13 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；6.8 mg/ml CHI 50 mM Na phosphate, pH 6.8. Precipitant 1.5 M (NH4)2SO4, 0.2 M NaCl, 0.1 M HEPES pH 7.5. Hanging drop 2+2 ul. soaking for 10 min in 2.5 mM taxifolin (2.5% ethanol)
Resolution 2.80 Å R-free 0.225
8B7Z Bacterial chalcone isomerase H33A with taxifolin Deposited 2022-10-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–283（283 aa）
Chain B 1–283（283 aa）
Chain K 1–283（283 aa）
Chain L 1–283（283 aa）
Chain M 1–283（283 aa）
Chain N 1–283（283 aa）
Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A DQH (2R,3R)-2-(3,4-DIHYDROXYPHENYL)-3,5,7-TRIHYDROXY-2,3-DIHYDRO-4H-CHROMEN-4-ONE × 16 GOL GLYCEROL × 1 SO4 SULFATE ION × 3 K POTASSIUM ION × 1 CL CHLORIDE ION × 6 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；6.8 mg/ml CHI 50 mM Na phosphate, pH 6.8. Precipitant 1.5 M (NH4)2SO4, 0.2 M NaCl, 0.1 M HEPES pH 7.5. Soaking for 10 min in 2.5 mM taxifolin (2.5% ethanol)
Resolution 3.00 Å R-free 0.268
8B7Z Bacterial chalcone isomerase H33A with taxifolin Deposited 2022-10-03 Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain C 1–283（283 aa）
Chain D 1–283（283 aa）
Chain E 1–283（283 aa）
Chain F 1–283（283 aa）
Chain G 1–283（283 aa）
Chain H 1–283（283 aa）
Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A DQH (2R,3R)-2-(3,4-DIHYDROXYPHENYL)-3,5,7-TRIHYDROXY-2,3-DIHYDRO-4H-CHROMEN-4-ONE × 12 SO4 SULFATE ION × 3 K POTASSIUM ION × 2 CL CHLORIDE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；6.8 mg/ml CHI 50 mM Na phosphate, pH 6.8. Precipitant 1.5 M (NH4)2SO4, 0.2 M NaCl, 0.1 M HEPES pH 7.5. Soaking for 10 min in 2.5 mM taxifolin (2.5% ethanol)
Resolution 3.00 Å R-free 0.268
8B7Z Bacterial chalcone isomerase H33A with taxifolin Deposited 2022-10-03 Assembly 3 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain I 1–283（283 aa）
Chain J 1–283（283 aa）
Chain O 1–283（283 aa）
Chain P 1–283（283 aa）
Chain Q 1–283（283 aa）
Chain R 1–283（283 aa）
Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A Mutation：H33A DQH (2R,3R)-2-(3,4-DIHYDROXYPHENYL)-3,5,7-TRIHYDROXY-2,3-DIHYDRO-4H-CHROMEN-4-ONE × 17 SO4 SULFATE ION × 2 CL CHLORIDE ION × 4 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；6.8 mg/ml CHI 50 mM Na phosphate, pH 6.8. Precipitant 1.5 M (NH4)2SO4, 0.2 M NaCl, 0.1 M HEPES pH 7.5. Soaking for 10 min in 2.5 mM taxifolin (2.5% ethanol)
Resolution 3.00 Å R-free 0.268

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.