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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：P46883 New Search
17PDB entries
17Biological assembly
34chain/assembly records
Main Difference Dimensions in This Set
Different construct 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
1D6U CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE Deposited 1999-10-15 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 31–757（727 aa）
Chain B 31–757（727 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 CA CALCIUM ION × 4 HY1 PHENYLACETALDEHYDE × 2 PEA 2-PHENYLETHYLAMINE × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；291 K；SODIUM CITRATE, HEPES BUFFER, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 18K
Resolution 2.40 Å R-free 0.239
1D6Y CRYSTAL STRUCTURE OF E. COLI COPPER-CONTAINING AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE AND COMPLEXED WITH NITRIC OXIDE. Deposited 1999-10-16 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 31–757（727 aa）
Chain B 31–757（727 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 CA CALCIUM ION × 4 HY1 PHENYLACETALDEHYDE × 2 NO NITRIC OXIDE × 2 PEA 2-PHENYLETHYLAMINE × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；291 K；sodium citrate, HEPES buffer, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 18K
Resolution 2.40 Å R-free 0.231
1D6Z CRYSTAL STRUCTURE OF THE AEROBICALLY FREEZE TRAPPED RATE-DETERMINING CATALYTIC INTERMEDIATE OF E. COLI COPPER-CONTAINING AMINE OXIDASE. Deposited 1999-10-16 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 31–757（727 aa）
Chain B 31–757（727 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 CA CALCIUM ION × 4 HY1 PHENYLACETALDEHYDE × 2 PEO HYDROGEN PEROXIDE × 2 PEA 2-PHENYLETHYLAMINE × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；291 K；sodium citrate, HEPES buffer, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 18K
Resolution 2.10 Å R-free 0.237
1DYU The active site base controls cofactor reactivity in Escherichia coli amine oxidase: X-ray crystallographic studies with mutational variants. Deposited 2000-02-08 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 31–757（727 aa）
Chain B 31–757（727 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.1；1.2 M SODIUM CITRATE, 0.1 M HEPES PH 7.1
Resolution 2.04 Å R-free 0.237
1JRQ X-ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. coli Amine Oxidase Deposited 2001-08-14 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 31–757（727 aa）
Chain B 31–757（727 aa）
Mutation：Y369F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y369F Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；291 K；SODIUM CITRATE, HEPES BUFFER, pH 7.40, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.15 Å R-free 0.235
1LVN CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE COMPLEXED WITH TRANYLCYPROMINE Deposited 2002-05-28 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 31–757（727 aa）
Chain B 31–757（727 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions Sitting drop；pH 7.2；291 K；1.3M SODIUM CITRATE, 0.1M HEPES BUFFER, pH 7.2, INHIBITOR SOAKING SOLUTION 10:1 RATIO OF RACEMIC TRANYLCYPROMINE TO ENZYME MADE UP IN 1.4M SODIUM CITRATE, 0.1M HEPES BUFFER, PH 7.2. CRYSTAL SOAKED FOR 20 DAYS.CRYOPROTECTANT 20% GLYCEROL, 1.4M SODIUM CITRATE BUFFER, PH 7.2, pH 7.20, Sitting drop, temperature 291.0K
Resolution 2.40 Å R-free 0.229
1OAC CRYSTAL STRUCTURE OF A QUINOENZYME: COPPER AMINE OXIDASE OF ESCHERICHIA COLI AT 2 ANGSTROEMS RESOLUTION Deposited 1995-09-27 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 31–757（727 aa）
Chain B 31–757（727 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 CA CALCIUM ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1QAF THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA COLI AMINE OXIDASE : X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL VARIANTS Deposited 1999-03-11 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 36–756（721 aa）
Chain B 36–756（721 aa）
Mutation：D383E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：D383E Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 CA CALCIUM ION × 4 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.1；315 K；VAPOR DIFFUSION, SITTING DROP PH 7.1, 315 K SODIUM CITRATE, HEPES
Resolution 2.20 Å R-free 0.244
1QAK THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA COLI AMINE OXIDASE : X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL VARIANTS Deposited 1999-03-15 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 36–757（722 aa）
Chain B 36–757（722 aa）
Mutation：D383A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：D383A Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.1；pH 7.1
Resolution 2.00 Å R-free 0.244
1QAL THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA COLI AMINE OXIDASE : X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL VARIANTS Deposited 1999-03-19 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 36–756（721 aa）
Chain B 36–756（721 aa）
Mutation：D383N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：D383N Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.1；315 K；VAPOR DIFFUSION, SITTING DROP, PH 7.1, 315K, 1.2 M SODIUM CITRATE, 0.1 M HEPES CRYOPROTECTANT 1.4 M SODIUM CITRATE 0.1M HEPES 20% GLYCEROL
Resolution 2.20 Å R-free 0.241
1SPU STRUCTURE OF OXIDOREDUCTASE Deposited 1996-11-13 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 31–757（727 aa）
Chain B 31–757（727 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.2；1.4M SODIUM CITRATE, 0.1M HEPES BUFFER, PH 7.2 PROTEIN SOLUTION CONCENTRATION 6.5 MG/ML INHIBITOR SOAKING SOLUTION 0.375MM 2-HYDRAZINOPYRIDINE MADE UP IN 1.4M SODIUM CITRATE, 0.1M HEPES BUFFER, PH 7.2. CRYSTAL SOAKED FOR 30 DAYS. CRYOPROTECTANT 20% GLYCEROL, 1.44M SODIUM CITRATE BUFFER, PH 6.4
Resolution 2.00 Å
2W0Q E. coli copper amine oxidase in complex with Xenon Deposited 2008-08-20 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 31–757（727 aa）
Chain B 31–757（727 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 CA CALCIUM ION × 4 XE XENON × 11 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.1；100MM HEPES, PH 7.1, 1.2 M SODIUM CITRATE
Resolution 2.48 Å R-free 0.219
2WGQ Zinc substituted E Coli Copper Amine Oxidase, a model for the precursor for 2,4,5-trihydroxyphenylalaninequinone formation Deposited 2009-04-23 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 31–757（727 aa）
Chain B 31–757（727 aa）
Not recorded ZN ZINC ION × 2 CA CALCIUM ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å R-free 0.264
2WO0 EDTA treated E. coli copper amine oxidase Deposited 2009-07-21 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 31–757（727 aa） Fragment：RESIDUES 31-757
Chain B 31–757（727 aa） Fragment：RESIDUES 31-757
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 NA SODIUM ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.60 Å R-free 0.248
2WOF EDTA treated E. coli copper amine oxidase Deposited 2009-07-23 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 31–757（727 aa）
Chain B 31–757（727 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 NA SODIUM ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.25 Å R-free 0.220
2WOH Strontium soaked E. coli copper amine oxidase Deposited 2009-07-23 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 31–757（727 aa）
Chain B 31–757（727 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 CA CALCIUM ION × 2 SR STRONTIUM ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.70 Å R-free 0.243
6EZZ Crystal structure of Escherichia coli amine oxidase mutant E573Q Deposited 2017-11-16 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 31–757（727 aa）
Chain B 31–757（727 aa）
Mutation：E573Q Mutation：E573Q CU COPPER (II) ION × 2 CA CALCIUM ION × 2 GOL GLYCEROL × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291.15 K；1.6 M Sodium citrate, 100mM HEPES pH 6-7
Resolution 1.80 Å R-free 0.197

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.