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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：P50477 New Search
11PDB entries
11Biological assembly
33chain/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
1CAU DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT Deposited 1993-07-08 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 44–224（181 aa）
Chain B 241–424（184 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.30 Å
1CAV THE THREE-DIMENSIONAL STRUCTURE OF CANAVALIN FROM JACK BEAN (CANAVALIA ENSIFORMIS) Deposited 1993-05-27 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 44–224（181 aa）
Chain B 241–424（184 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.60 Å
1CAW DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT Deposited 1993-06-02 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 44–224（181 aa）
Chain B 241–424（184 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.60 Å
1CAX DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT Deposited 1993-06-10 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 44–224（181 aa）
Chain B 241–424（184 aa）
Chain C 44–224（181 aa）
Chain D 241–424（184 aa）
Chain E 44–224（181 aa）
Chain F 241–424（184 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.60 Å
1DGR Refined crystal structure of canavalin from jack bean Deposited 1999-11-25 Assembly 1 Protein homooligomer Homooligomer；Protein × 9 PDB declaration: nonameric（9） Consistent with protein count
Chain A 46–223（178 aa） Fragment：RESIDUES 46-223
Chain B 46–223（178 aa） Fragment：RESIDUES 46-223
Chain C 46–223（178 aa） Fragment：RESIDUES 46-223
Chain M 331–423（93 aa） Fragment：RESIDUES 331-423
Chain N 246–324（79 aa） Fragment：RESIDUES 246-324
Chain V 246–324（79 aa） Fragment：RESIDUES 246-324
Chain W 331–423（93 aa） Fragment：RESIDUES 331-423
Chain X 246–324（79 aa） Fragment：RESIDUES 246-324
Chain Y 331–423（93 aa） Fragment：RESIDUES 331-423
Not recorded PO4 PHOSPHATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.8；277 K；Dulbeccos phosphate buffered saline, ammonium hydroxide, pH 6.8, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.60 Å R-free 0.226
1DGW Structure of the rhombohedral crystal of canavalin from jack bean Deposited 1999-11-26 Assembly 1 Protein homooligomer Homooligomer；Protein × 9 PDB declaration: nonameric（9） Consistent with protein count
Chain A 46–223（178 aa） Fragment：RESIDUES 46-223
Chain X 246–324（79 aa） Fragment：RESIDUES 246-324
Chain Y 331–423（93 aa） Fragment：RESIDUES 331-423
Not recorded PO4 PHOSPHATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions LIQUID DIFFUSION；pH 6.8；293 K；DULBECCO'S PHOSPHATE BUFFERED SALINE, AMMONIUM HYDROXIDE (TRACE), MICROGRAVITY, pH 6.8, LIQUID DIFFUSION, temperature 293K
Resolution 1.70 Å R-free 0.252
2CAU CANAVALIN FROM JACK BEAN Deposited 1998-11-20 Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 1–445（445 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.8；THIS CRYSTAL FORM COULD BE GROWN ONLY OCCASIONALLY. BASICALLY IT WAS CRYSTALLIZED FROM PURIFIED PROTEIN AFTER TRYPSIN TREATMENT IN PHOSPHATE BUFFERED SALINE, BUT WAS DIFFICULT TO REPRODUCE., pH 6.8
Resolution 2.10 Å R-free 0.235
2CAV CANAVALIN FROM JACK BEAN Deposited 1998-11-20 Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 1–445（445 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.8；30 - 40 MG/ML PROTEIN SOLUTION WAS PREPARED BY DISSOLVING 4-TIME RECRYSTALLIZED CANAVALIN IN DISTILLED WATER PLUS TRACE NH4OH. RESERVOIR SOLUTION CONTAINED 2.0 % NACL IN 50 MM PHOSPHATE BUFFER AT PH 6.8. CRYSTALS WERE OBTAINED BY MIXING PROTEIN AND RESERVOIR SOLUTION IN SITTING DROPS FOLLOWED BY VAPOR DIFFUSION AGAINST THE RESERVOIR., vapor diffusion
Resolution 2.00 Å R-free 0.264
6V7G Binding of Benzoic Acid and Anions Within the Cupin Domains of the Vicillin Protein Canavalin from Jack Bean (canavalia ensiformis): Crystal Structures Deposited 2019-12-08 Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 1–445（445 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ACT ACETATE ION × 3 BEZ BENZOIC ACID × 3 CIT CITRIC ACID × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；Vapor diffusion in sitting drop Cryschem plates. Reservoirs were 1.0 M sodium citrate titrated with acetic acid to pH6.0. Drops were initially equal amounts of the reservoir solution with a protein stock solution of 30 mg/ml canavalin in water with a trace of ammonium hydroxide. At room temperature crystallization time was about three weeks.
Resolution 1.40 Å R-free 0.188
6V7J The C2221 crystal form of canavalin at 173 K Deposited 2019-12-08 Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 1–445（445 aa）
Chain B 1–445（445 aa）
Chain C 1–445（445 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) BEZ BENZOIC ACID × 3 GOL GLYCEROL × 3 CA CALCIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；Vapor diffusion in Cryschem sitting drop plates at room temperature. Reservoirs were Dulbeccos Phosphate buffered saline at pH 6.5. Drops were equal amounts of the reservoir and a 40 mg/ml solution of the protein dissolved in water with a trace of ammonium hydroxide. Crystallization time was 24 to 48 hours.
Resolution 2.00 Å R-free 0.247
6V7L The structure of the P212121 crystal form of canavalin at 173 K Deposited 2019-12-08 Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 1–445（445 aa）
Chain B 1–445（445 aa）
Chain C 1–445（445 aa）
Not recorded BEZ BENZOIC ACID × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；298 K；Crystals were grown by sitting drop vapor diffusion from 18% PEG 3350 in 0.1 M HEPES reservoirs. The drops were equal amounts of a 40 mg/ml solution of precanavalin (not treated with any exogenous protease) in water. Crystals grew only after six to eight weeks at room temperature.
Resolution 2.80 Å R-free 0.252

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.