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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：P20231 New Search
11PDB entries
12Biological assembly
42chain/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
1A0L HUMAN BETA-TRYPTASE: A RING-LIKE TETRAMER WITH ACTIVE SITES FACING A CENTRAL PORE Deposited 1997-12-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 31–274（244 aa）
Chain B 31–274（244 aa）
Chain C 31–274（244 aa）
Chain D 31–274（244 aa）
Not recorded APA (2S)-3-(4-carbamimidoylphenyl)-2-hydroxypropanoic acid × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5；pH 5.0
Resolution 3.00 Å R-free 0.276
2BM2 human beta-II tryptase in complex with 4-(3-Aminomethyl-phenyl)- piperidin-1-yl-(5-phenethyl- pyridin-3-yl)-methanone Deposited 2005-03-09 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 31–275（245 aa）
Chain B 31–275（245 aa）
Chain C 31–275（245 aa）
Chain D 31–275（245 aa）
Not recorded PM2 1-[3-(1-{[5-(2-PHENYLETHYL)PYRIDIN-3-YL]CARBONYL}PIPERIDIN-4-YL)PHENYL]METHANAMINE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions 291 K；PEG 3000 13-19%. NA.ACETATE 100 MM PH 5. T=18 DEG C. TAKES ABOUT 3 DAYS TO GET 200 MICROMETRE SILEX SHAPED CRYSTALS
Resolution 2.20 Å R-free 0.259
2FPZ Human tryptase with 2-amino benzimidazole Deposited 2006-01-17 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 31–275（245 aa）
Chain B 31–275（245 aa）
Chain C 31–275（245 aa）
Chain D 31–275（245 aa）
Not recorded AX7 1H-benzimidazol-2-amine × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；281 K；0.1M sodium acetate, 0.2M ammonium sulfate, 30% PEG 1500, pH 4.6, VAPOR DIFFUSION, temperature 281K
Resolution 2.00 Å R-free 0.240
2FS8 Human beta-tryptase II with inhibitor CRA-29382 Deposited 2006-01-21 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 31–275（245 aa）
Chain B 31–275（245 aa）
Chain C 31–275（245 aa）
Chain D 31–275（245 aa）
Not recorded C3A ALLYL {(1S)-1-[(5-{4-[(2,3-DIHYDRO-1H-INDEN-2-YLAMINO)CARBONYL]BENZYL}-1,2,4-OXADIAZOL-3-YL)CARBONYL]-3-PYRROLIDIN-3-YLPROPYL}CARBAMATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；2mg/mL protein in 10mM MES, pH 6.1, 2M NaCl mixed in reservoir solution containing 0.1 M NaOAc, pH 4.6, 0.2 M ammonium sulfate, 30% PEG 1500. Crystallization drops were set up using various ratios of protein solution to crystallization solution. Crystals appropriate for diffraction studies appeared in 2-5 days at room temperature, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K
Resolution 2.50 Å R-free 0.250
2FS9 Human beta tryptase II with inhibitor CRA-28427 Deposited 2006-01-21 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 31–275（245 aa）
Chain B 31–275（245 aa）
Chain C 31–275（245 aa）
Chain D 31–275（245 aa）
Not recorded C4A ETHYL {(1S)-5-AMINO-1-[(5-{4-[(2,3-DIHYDRO-1H-INDEN-2-YLAMINO)CARBONYL]BENZYL}-1,2,4-OXADIAZOL-3-YL)CARBONYL]PENTYL}CARBAMATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；2mg/mL protein in 10mM MES, pH 6.1, 2M NaCl mixed with reservoir solution containing 0.1 M NaOAc, pH 4.6, 0.2 M ammonium sulfate, 30% PEG 1500. Crystallization drops were set up using various ratios of protein solution to crystallization solution. Crystals appropriate for diffraction studies appeared in 2-5 days at room temperature, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K
Resolution 2.30 Å R-free 0.254
2FWW human beta-tryptase II complexed with 4-piperidinebutyrate to make acylenzyme Deposited 2006-02-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 31–275（245 aa）
Chain B 31–275（245 aa）
Chain C 31–275（245 aa）
Chain D 31–275（245 aa）
Not recorded C1R 4-PIPERIDINEBUTYRATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions 293 K；2mg/mL of protein, 10 mM MES, pH 6.1, 2M NaCl was mixed with crystallization solution 0.1 M NaOAc, pH 4.6, 0.2 M ammonium sulfate, 30% PEG 1500. Crystallization drops were set up using various ratios of protein solution to crystallization solution. Crystals appropriate for diffraction studies appeared in 2-5 days at room temperature, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K
Resolution 2.25 Å R-free 0.257
2FXR human beta tryptase II complexed with activated ketone inhibitor CRA-29382 Deposited 2006-02-06 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 31–275（245 aa）
Chain B 31–275（245 aa）
Chain C 31–275（245 aa）
Chain D 31–275（245 aa）
Not recorded C3A ALLYL {(1S)-1-[(5-{4-[(2,3-DIHYDRO-1H-INDEN-2-YLAMINO)CARBONYL]BENZYL}-1,2,4-OXADIAZOL-3-YL)CARBONYL]-3-PYRROLIDIN-3-YLPROPYL}CARBAMATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；2mg/mL protein, 10 mM MES, pH 6.1, 2M NaCl dissolved in 0.1 M NaOAc, pH 4.6, 0.2 M ammonium sulfate, 30% PEG 1500. Crystallization drops were set up using various ratios of protein solution to crystallization solution. Crystals appropriate for diffraction studies appeared in 2-5 days at room temperature, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K
Resolution 2.50 Å R-free 0.259
2GDD Human beta II tryptase with inhibitor CRA-27592 Deposited 2006-03-15 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 31–275（245 aa）
Chain B 31–275（245 aa）
Chain C 31–275（245 aa）
Chain D 31–275（245 aa）
Not recorded 5AM BENZYL {(1S)-5-AMINO-1-[(S)-HYDROXY(5-{[4-(4-PHENYLBUTANOYL)PIPERAZIN-1-YL]METHYL}-1,2,4-OXADIAZOL-3-YL)METHYL]PENTYL}CARBAMATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；293 K；Tryptase was purchased from Promega (catalog #G563X). The protein was formulated as a 2 mg/mL solution in 10 mM MES (pH 6.1) and 2M NaCl, and was crystallized from a solution of 0.1 M NaoAc (pH 4.6), 0.2 M ammonium sulfate and 30% PEG 1500 (all reagents obtained from Hampton Research). Crystallization drops were set up at various ratios of protein solution to crystallization solution. Crystals appeared in 2-5 days at room temperature., VAPOR DIFFUSION, temperature 293.0K
Resolution 2.35 Å R-free 0.254
5F03 TRYPTASE B2 IN COMPLEX WITH 5-(3-Aminomethyl-phenoxymethyl)-3-[3-(2-chloro-pyridin-3-ylethynyl)-phenyl]-oxazolidin-2-one; compound with trifluoro-acetic acid Deposited 2015-11-27 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 31–275（245 aa）
Mutation：NO 5TA (5~{S})-5-[[3-(aminomethyl)phenoxy]methyl]-3-[3-[2-(2-chloranylpyridin-3-yl)ethynyl]phenyl]-1,3-oxazolidin-2-one × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；20% PEG 10000, 0.1 M HEPES
Resolution 1.94 Å R-free 0.200
5F03 TRYPTASE B2 IN COMPLEX WITH 5-(3-Aminomethyl-phenoxymethyl)-3-[3-(2-chloro-pyridin-3-ylethynyl)-phenyl]-oxazolidin-2-one; compound with trifluoro-acetic acid Deposited 2015-11-27 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 31–275（245 aa）
Mutation：NO 5TA (5~{S})-5-[[3-(aminomethyl)phenoxy]methyl]-3-[3-[2-(2-chloranylpyridin-3-yl)ethynyl]phenyl]-1,3-oxazolidin-2-one × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；20% PEG 10000, 0.1 M HEPES
Resolution 1.94 Å R-free 0.200
9QFU Human Tryptase beta-2 (hTPSB2) complexed with covalent inhibitor Compound #1 Deposited 2025-03-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 31–273（243 aa）
Chain B 31–273（243 aa）
Chain C 31–273（243 aa）
Chain D 31–273（243 aa）
Not recorded A1I52 ~{N}-[(1~{S},2~{S})-6-azanyl-1-[5-[[4-[2-(3,4-dichlorophenyl)ethoxy]phenyl]methyl]-1,2,4-oxadiazol-3-yl]-1-oxidanyl-hexan-2-yl]-4-fluoranyl-benzamide × 4 SO4 SULFATE ION × 16 PEG DI(HYDROXYETHYL)ETHER × 2 EDO 1,2-ETHANEDIOL × 15 ACT ACETATE ION × 3 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；The protein was formulated as a 2 mg/mL solution in 10 mM MES (pH 6.1) and 2M NaCl, and was crystallized from a solution of 0.1 M NaoAc (pH 4.6), 0.2 M ammonium sulfate and 30% PEG 1500
Resolution 1.98 Å R-free 0.221
9QFV Human Tryptase beta-2 (hTPSB2) Deposited 2025-03-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 31–275（245 aa）
Chain B 31–275（245 aa）
Chain C 31–275（245 aa）
Chain D 31–275（245 aa）
Not recorded ACT ACETATE ION × 4 EDO 1,2-ETHANEDIOL × 13 SO4 SULFATE ION × 8 GOL GLYCEROL × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 4 1PE PENTAETHYLENE GLYCOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；293 K；The protein was formulated as a 2 mg/mL solution in 10 mM MES (pH 6.1) and 2M NaCl, and was crystallized from a solution of 0.1 M NaoAc (pH 4.6), 0.2 M ammonium sulfate and 30% PEG 1500
Resolution 2.06 Å R-free 0.219

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.