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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：P30074 New Search
16PDB entries
18Biological assembly
27chain/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
1BI5 CHALCONE SYNTHASE FROM ALFALFA Deposited 1998-06-22 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–389（389 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 1.56 Å R-free 0.193
1BQ6 CHALCONE SYNTHASE FROM ALFALFA WITH COENZYME A Deposited 1998-08-21 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 2–389（388 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 2 COA COENZYME A × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 1.56 Å R-free 0.212
1CGK CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH NARINGENIN Deposited 1999-03-25 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–389（389 aa）
Not recorded NAR NARINGENIN × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；THE DROPLE CONSISTED ON 25 MGR/ML (FINAL CONCENTRATION) PROTEIN MIXED WITH THE RESERVOIR WHICH CONTAINED 2.4 M AMMONIUM SULFATE, 100 MM PIPES BUFFER (PH 6.5) , IN THE PRESENCE (UP TO 5 MM) OR ABSENCE OF DTT REDUCING AGENT. CRYSTALS WERE STABILIZED IN 40% (V/V) PEG400, 100 MM PIPES 16 MM NARINGENIN PRIOR TO FREEZING AT 105 K, pH 6.50
Resolution 1.84 Å R-free 0.225
1CGZ CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH RESVERATROL Deposited 1999-03-26 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–389（389 aa）
Not recorded STL RESVERATROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.50
Resolution 1.70 Å R-free 0.217
1CHW CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH HEXANOYL-COA Deposited 1999-03-30 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–389（389 aa）
Chain B 1–389（389 aa）
Mutation：C164S Mutation：C164S HXC HEXANOYL-COENZYME A × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；THE CRYSTALS WERE OBTAINED OVERNIGHT AT 4 C HANGING-DROP VAPOR DIFFUSION METHOD. THE DROPLET CONSISTED ON 25 MGR/ML (FINAL CONCENTRATION) PROTEIN MIXED WITH THE RESERVOIR WHICH CONTAINED 2.4 M AMMONIUM SULFATE, 100 MM PIPES BUFFER (PH 6.5), IN THE PRESENCE (UP TO 5 MM) OR ABSENCE OF DTT REDUCING AGENT. CRYSTALS WERE STABILIZED IN 40% (V/V) PEG400, 100 MM PIPES AND 20 MM HEXANOYL-COA PRIOR TO FREEZING AT 105 K.
Resolution 1.90 Å R-free 0.290
1CML CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH MALONYL-COA Deposited 1999-03-30 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–389（389 aa）
Mutation：C164A SO4 SULFATE ION × 2 MLC MALONYL-COENZYME A × 2 PIN PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID) × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.50
Resolution 1.69 Å R-free 0.200
1D6F CHALCONE SYNTHASE C164A MUTANT Deposited 1999-10-13 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–389（389 aa）
Mutation：C164A SO4 SULFATE ION × 2 B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PROPANE, 2 MM DITHIOTHREITOL (DTT), pH 6.5, VAPOR DIFFUSION, HANGING DROP
Resolution 1.69 Å R-free 0.201
1D6H CHALONE SYNTHASE (N336A MUTANT COMPLEXED WITH COA) Deposited 1999-10-13 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 3–389（387 aa）
Mutation：N336A Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 2 COA COENZYME A × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PROPANE, 2 MM DITHIOTHREITOL (DTT), pH 6.5, VAPOR DIFFUSION, HANGING DROP
Resolution 2.15 Å R-free 0.257
1D6I CHALCONE SYNTHASE (H303Q MUTANT) Deposited 1999-10-13 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 2–389（388 aa） Fragment：CHS
Chain B 2–389（388 aa） Fragment：CHS
Mutation：H303Q Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：H303Q Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PROPANE, 2 MM DITHIOTHREITOL (DTT), pH 6.5, VAPOR DIFFUSION, HANGING DROP
Resolution 2.00 Å R-free 0.269
1D6I CHALCONE SYNTHASE (H303Q MUTANT) Deposited 1999-10-13 Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 2–389（388 aa） Fragment：CHS
Chain B 2–389（388 aa） Fragment：CHS
Mutation：H303Q Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：H303Q Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PROPANE, 2 MM DITHIOTHREITOL (DTT), pH 6.5, VAPOR DIFFUSION, HANGING DROP
Resolution 2.00 Å R-free 0.269
1I86 CHALCONE SYNTHASE, G256A MUTANT Deposited 2001-03-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–389（389 aa）
Mutation：CHALCONE SYNTHASE (G256A) Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M ammonium sulfate, 100 mM PIPES, 5 mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.50 Å R-free 0.221
1I88 CHALCONE SYNTHASE (G256V) Deposited 2001-03-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–389（389 aa）
Chain B 1–389（389 aa）
Mutation：G256V Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：G256V Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M ammonium sulfate, 0.1 M PIPES, 5 mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.45 Å R-free 0.221
1I89 Chalcone synthase (G256L) Deposited 2001-03-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–389（389 aa）
Chain B 1–389（389 aa）
Mutation：G256L Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：G256L Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M ammonium sulfate, 0.1 M PIPES, 5 mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.86 Å R-free 0.259
1I8B Chalcone synthase (G256F) Deposited 2001-03-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–389（389 aa）
Chain B 1–389（389 aa）
Mutation：G256F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：G256F Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M ammonium sulfate, 0.1 M PIPES, 5 mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.95 Å R-free 0.251
1JWX Chalcone Synthase--F215S mutant Deposited 2001-09-05 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–389（389 aa）
Mutation：F215S Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；ammonium sulfate, PIPES, DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.63 Å R-free 0.225
1U0V An Aldol Switch Discovered in Stilbene Synthases Mediates Cyclization of Specificity of Type III Polyketide Synthases: 18xCHS structure Deposited 2004-07-14 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–389（389 aa）
Chain B 1–389（389 aa）
Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG 8000, ammonium acetate, HEPES-Na+ buffer, ethylene glycol, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.90 Å R-free 0.227
1U0W An Aldol Switch Discovered in Stilbene Synthases Mediates Cyclization Specificity of Type III Polyketide Synthases: 18xCHS+resveratrol Structure Deposited 2004-07-14 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–389（389 aa）
Chain B 1–389（389 aa）
Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D STL RESVERATROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG 8000, ammonium acetate, HEPES-Na+ buffer, ethylene glycol, resveratrol, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.00 Å R-free 0.264
1U0W An Aldol Switch Discovered in Stilbene Synthases Mediates Cyclization Specificity of Type III Polyketide Synthases: 18xCHS+resveratrol Structure Deposited 2004-07-14 Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 1–389（389 aa）
Chain D 1–389（389 aa）
Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D STL RESVERATROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG 8000, ammonium acetate, HEPES-Na+ buffer, ethylene glycol, resveratrol, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.00 Å R-free 0.264

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.