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1a2v

COPPER AMINE OXIDASE FROM HANSENULA POLYMORPHA

Method: X-RAY DIFFRACTION Dmax: 139.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

METHYLAMINE OXIDASE

Pichia angusta

UniProt P12807

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count Chain A； UniProt 18–672 Chain B； UniProt 18–672 Chain C； UniProt 18–672 Chain D； UniProt 18–672 Chain E； UniProt 18–672 Chain F； UniProt 18–672 Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.2；PROTEIN WAS CRYSTALLIZED IN SITTING DROPS FROM 7-9% PEG 8000 AND 0.3 M POTASSIUM PHOSPHATE BUFFER, PH 6.2 Resolution 2.40 Å R-free 0.224

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 1A2V Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1EKM CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI Deposited 2000-03-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 17–672（656 aa）
Chain B 17–672（656 aa）
Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；PEG 8000, potassium phosphate, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
Resolution 2.50 Å R-free 0.208
1EKM CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI Deposited 2000-03-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 17–672（656 aa）
Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；PEG 8000, potassium phosphate, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
Resolution 2.50 Å R-free 0.208
1EKM CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI Deposited 2000-03-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 17–672（656 aa）
Chain B 17–672（656 aa）
Chain C 17–672（656 aa）
Not recorded ZN ZINC ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；PEG 8000, potassium phosphate, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
Resolution 2.50 Å R-free 0.208
2OOV Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms Deposited 2007-01-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 13–672（660 aa） Fragment：Residues 13-672
Chain B 13–672（660 aa） Fragment：Residues 13-672
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 GOL GLYCEROL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG 8000, 0.3M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 1.70 Å R-free 0.178
2OOV Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms Deposited 2007-01-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 13–672（660 aa） Fragment：Residues 13-672
Chain D 13–672（660 aa） Fragment：Residues 13-672
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 GOL GLYCEROL × 6 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG 8000, 0.3M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 1.70 Å R-free 0.178
2OOV Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms Deposited 2007-01-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 13–672（660 aa） Fragment：Residues 13-672
Chain F 13–672（660 aa） Fragment：Residues 13-672
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 GOL GLYCEROL × 10 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG 8000, 0.3M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 1.70 Å R-free 0.178
2OOV Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms Deposited 2007-01-26 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 13–672（660 aa） Fragment：Residues 13-672
Chain B 13–672（660 aa） Fragment：Residues 13-672
Chain C 13–672（660 aa） Fragment：Residues 13-672
Chain D 13–672（660 aa） Fragment：Residues 13-672
Chain E 13–672（660 aa） Fragment：Residues 13-672
Chain F 13–672（660 aa） Fragment：Residues 13-672
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) 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) CU COPPER (II) ION × 6 GOL GLYCEROL × 28 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG 8000, 0.3M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 1.70 Å R-free 0.178
2OQE Crystal Structure of Hansenula polymorpha amine oxidase in complex with Xe to 1.6 Angstroms Deposited 2007-01-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 13–672（660 aa） Fragment：residues 13-672
Chain B 13–672（660 aa） Fragment：residues 13-672
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 XE XENON × 8 GOL GLYCEROL × 20 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8% PEG 8000, 0.3M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K, pH 6.00
Resolution 1.60 Å R-free 0.188
2OQE Crystal Structure of Hansenula polymorpha amine oxidase in complex with Xe to 1.6 Angstroms Deposited 2007-01-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 13–672（660 aa） Fragment：residues 13-672
Chain D 13–672（660 aa） Fragment：residues 13-672
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 XE XENON × 8 GOL GLYCEROL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8% PEG 8000, 0.3M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K, pH 6.00
Resolution 1.60 Å R-free 0.188
2OQE Crystal Structure of Hansenula polymorpha amine oxidase in complex with Xe to 1.6 Angstroms Deposited 2007-01-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 13–672（660 aa） Fragment：residues 13-672
Chain F 13–672（660 aa） Fragment：residues 13-672
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 XE XENON × 8 GOL GLYCEROL × 17 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8% PEG 8000, 0.3M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K, pH 6.00
Resolution 1.60 Å R-free 0.188
2OQE Crystal Structure of Hansenula polymorpha amine oxidase in complex with Xe to 1.6 Angstroms Deposited 2007-01-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 13–672（660 aa） Fragment：residues 13-672
Chain B 13–672（660 aa） Fragment：residues 13-672
Chain E 13–672（660 aa） Fragment：residues 13-672
Chain F 13–672（660 aa） Fragment：residues 13-672
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) Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 4 XE XENON × 16 GOL GLYCEROL × 37 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8% PEG 8000, 0.3M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K, pH 6.00
Resolution 1.60 Å R-free 0.188
2OQE Crystal Structure of Hansenula polymorpha amine oxidase in complex with Xe to 1.6 Angstroms Deposited 2007-01-31 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 13–672（660 aa） Fragment：residues 13-672
Chain B 13–672（660 aa） Fragment：residues 13-672
Chain C 13–672（660 aa） Fragment：residues 13-672
Chain D 13–672（660 aa） Fragment：residues 13-672
Chain E 13–672（660 aa） Fragment：residues 13-672
Chain F 13–672（660 aa） Fragment：residues 13-672
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) 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) CU COPPER (II) ION × 6 XE XENON × 24 GOL GLYCEROL × 49 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8% PEG 8000, 0.3M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K, pH 6.00
Resolution 1.60 Å R-free 0.188
3N9H Crystal Structural of mutant Y305A in the copper amine oxidase from hansenula polymorpha Deposited 2010-05-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Mutation：Y305A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305A Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.3；295 K；10% PEG8000. 0.125M Lithium sulfate and 0.1M KPi, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.50 Å R-free 0.198
3N9H Crystal Structural of mutant Y305A in the copper amine oxidase from hansenula polymorpha Deposited 2010-05-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 1–692（692 aa）
Chain D 1–692（692 aa）
Mutation：Y305A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305A Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.3；295 K；10% PEG8000. 0.125M Lithium sulfate and 0.1M KPi, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.50 Å R-free 0.198
3N9H Crystal Structural of mutant Y305A in the copper amine oxidase from hansenula polymorpha Deposited 2010-05-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 1–692（692 aa）
Chain F 1–692（692 aa）
Mutation：Y305A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305A Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.3；295 K；10% PEG8000. 0.125M Lithium sulfate and 0.1M KPi, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.50 Å R-free 0.198
3N9H Crystal Structural of mutant Y305A in the copper amine oxidase from hansenula polymorpha Deposited 2010-05-30 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Chain C 1–692（692 aa）
Chain D 1–692（692 aa）
Chain E 1–692（692 aa）
Chain F 1–692（692 aa）
Mutation：Y305A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305A Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.3；295 K；10% PEG8000. 0.125M Lithium sulfate and 0.1M KPi, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.50 Å R-free 0.198
3NBB Crystal structure of mutant Y305F expressed in E. coli in the copper amine oxidase from hansenula polymorpha Deposited 2010-06-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；295 K；20% PEG8000, 100mM HEPES, 2% ethylene glycol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.05 Å R-free 0.200
3NBB Crystal structure of mutant Y305F expressed in E. coli in the copper amine oxidase from hansenula polymorpha Deposited 2010-06-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 1–692（692 aa）
Chain D 1–692（692 aa）
Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；295 K；20% PEG8000, 100mM HEPES, 2% ethylene glycol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.05 Å R-free 0.200
3NBB Crystal structure of mutant Y305F expressed in E. coli in the copper amine oxidase from hansenula polymorpha Deposited 2010-06-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 1–692（692 aa）
Chain F 1–692（692 aa）
Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；295 K；20% PEG8000, 100mM HEPES, 2% ethylene glycol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.05 Å R-free 0.200
3NBB Crystal structure of mutant Y305F expressed in E. coli in the copper amine oxidase from hansenula polymorpha Deposited 2010-06-03 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Chain C 1–692（692 aa）
Chain D 1–692（692 aa）
Chain E 1–692（692 aa）
Chain F 1–692（692 aa）
Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；295 K；20% PEG8000, 100mM HEPES, 2% ethylene glycol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.05 Å R-free 0.200
3NBJ Crystal Structure of Y305F mutant of the copper amine oxidase from Hansenula polymorpha expressed in yeast Deposited 2010-06-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 PO4 PHOSPHATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；295 K；8% PEG8000, 200mM KPi, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.90 Å R-free 0.217
3NBJ Crystal Structure of Y305F mutant of the copper amine oxidase from Hansenula polymorpha expressed in yeast Deposited 2010-06-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 1–692（692 aa）
Chain D 1–692（692 aa）
Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 PO4 PHOSPHATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；295 K；8% PEG8000, 200mM KPi, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.90 Å R-free 0.217
3NBJ Crystal Structure of Y305F mutant of the copper amine oxidase from Hansenula polymorpha expressed in yeast Deposited 2010-06-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 1–692（692 aa）
Chain F 1–692（692 aa）
Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 PO4 PHOSPHATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；295 K；8% PEG8000, 200mM KPi, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.90 Å R-free 0.217
3NBJ Crystal Structure of Y305F mutant of the copper amine oxidase from Hansenula polymorpha expressed in yeast Deposited 2010-06-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Chain C 1–692（692 aa）
Chain D 1–692（692 aa）
Chain E 1–692（692 aa）
Chain F 1–692（692 aa）
Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y305F Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 6 PO4 PHOSPHATE ION × 18 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；295 K；8% PEG8000, 200mM KPi, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.90 Å R-free 0.217
3SX1 Hansenula polymorpha copper amine oxidase-1 in its apo form Deposited 2011-07-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–692（692 aa）
Not recorded GOL GLYCEROL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG 8000, 0.28 M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.73 Å R-free 0.163
3SX1 Hansenula polymorpha copper amine oxidase-1 in its apo form Deposited 2011-07-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 1–692（692 aa）
Chain C 1–692（692 aa）
Not recorded GOL GLYCEROL × 8 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG 8000, 0.28 M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.73 Å R-free 0.163
3SX1 Hansenula polymorpha copper amine oxidase-1 in its apo form Deposited 2011-07-14 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Chain C 1–692（692 aa）
Not recorded GOL GLYCEROL × 28 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG 8000, 0.28 M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.73 Å R-free 0.163
3SXX Hansenula polymorpha copper amine oxidase-1 in complex with Co(II) Deposited 2011-07-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Not recorded CO COBALT (II) ION × 2 GOL GLYCEROL × 18 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8.5% PEG 8000, 0.27 M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.27 Å R-free 0.138
3SXX Hansenula polymorpha copper amine oxidase-1 in complex with Co(II) Deposited 2011-07-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 1–692（692 aa）
Chain D 1–692（692 aa）
Not recorded CO COBALT (II) ION × 2 GOL GLYCEROL × 13 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8.5% PEG 8000, 0.27 M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.27 Å R-free 0.138
3SXX Hansenula polymorpha copper amine oxidase-1 in complex with Co(II) Deposited 2011-07-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 1–692（692 aa）
Chain F 1–692（692 aa）
Not recorded CO COBALT (II) ION × 2 GOL GLYCEROL × 12 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8.5% PEG 8000, 0.27 M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.27 Å R-free 0.138
3SXX Hansenula polymorpha copper amine oxidase-1 in complex with Co(II) Deposited 2011-07-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Chain C 1–692（692 aa）
Chain D 1–692（692 aa）
Chain E 1–692（692 aa）
Chain F 1–692（692 aa）
Not recorded CO COBALT (II) ION × 6 GOL GLYCEROL × 43 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8.5% PEG 8000, 0.27 M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.27 Å R-free 0.138
3T0U Hansenula polymorpha copper amine oxidase-1 in complex with Cu(I) Deposited 2011-07-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Not recorded CU1 COPPER (I) ION × 2 GOL GLYCEROL × 11 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8% PEG 8000, 0.28 M potassium phosphate pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.90 Å R-free 0.168
3T0U Hansenula polymorpha copper amine oxidase-1 in complex with Cu(I) Deposited 2011-07-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 1–692（692 aa）
Not recorded CU1 COPPER (I) ION × 2 GOL GLYCEROL × 16 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8% PEG 8000, 0.28 M potassium phosphate pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.90 Å R-free 0.168
3T0U Hansenula polymorpha copper amine oxidase-1 in complex with Cu(I) Deposited 2011-07-20 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Chain C 1–692（692 aa）
Not recorded CU1 COPPER (I) ION × 6 GOL GLYCEROL × 38 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8% PEG 8000, 0.28 M potassium phosphate pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.90 Å R-free 0.168
4EV2 Crystal structure of copper amine oxidase-1 from Hansenula polymorpha in complex with ethylamine Deposited 2012-04-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) GOL GLYCEROL × 12 CU COPPER (II) ION × 2 PEO HYDROGEN PEROXIDE × 2 NEH ETHANAMINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG8000, 0.22 M potassium phosphate, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.18 Å R-free 0.201
4EV2 Crystal structure of copper amine oxidase-1 from Hansenula polymorpha in complex with ethylamine Deposited 2012-04-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 1–692（692 aa）
Chain D 1–692（692 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) GOL GLYCEROL × 10 CU COPPER (II) ION × 2 NEH ETHANAMINE × 2 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG8000, 0.22 M potassium phosphate, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.18 Å R-free 0.201
4EV2 Crystal structure of copper amine oxidase-1 from Hansenula polymorpha in complex with ethylamine Deposited 2012-04-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 1–692（692 aa）
Chain F 1–692（692 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) GOL GLYCEROL × 9 CU COPPER (II) ION × 2 PEO HYDROGEN PEROXIDE × 2 NEH ETHANAMINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG8000, 0.22 M potassium phosphate, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.18 Å R-free 0.201
4EV2 Crystal structure of copper amine oxidase-1 from Hansenula polymorpha in complex with ethylamine Deposited 2012-04-25 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Chain C 1–692（692 aa）
Chain D 1–692（692 aa）
Chain E 1–692（692 aa）
Chain F 1–692（692 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) 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) GOL GLYCEROL × 31 CU COPPER (II) ION × 6 PEO HYDROGEN PEROXIDE × 4 NEH ETHANAMINE × 6 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG8000, 0.22 M potassium phosphate, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.18 Å R-free 0.201
4EV5 Crystal structure of copper amine oxidase-1 from Hansenula polymorpha in complex with benzylamine Deposited 2012-04-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) GOL GLYCEROL × 11 CU COPPER (II) ION × 2 PEO HYDROGEN PEROXIDE × 2 ABN BENZYLAMINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG8000, 0.22 M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.25 Å R-free 0.230
4EV5 Crystal structure of copper amine oxidase-1 from Hansenula polymorpha in complex with benzylamine Deposited 2012-04-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 1–692（692 aa）
Chain D 1–692（692 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) GOL GLYCEROL × 10 CU COPPER (II) ION × 2 ABN BENZYLAMINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG8000, 0.22 M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.25 Å R-free 0.230
4EV5 Crystal structure of copper amine oxidase-1 from Hansenula polymorpha in complex with benzylamine Deposited 2012-04-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 1–692（692 aa）
Chain F 1–692（692 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) GOL GLYCEROL × 9 CU COPPER (II) ION × 2 PEO HYDROGEN PEROXIDE × 2 ABN BENZYLAMINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG8000, 0.22 M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.25 Å R-free 0.230
4EV5 Crystal structure of copper amine oxidase-1 from Hansenula polymorpha in complex with benzylamine Deposited 2012-04-25 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–692（692 aa）
Chain B 1–692（692 aa）
Chain C 1–692（692 aa）
Chain D 1–692（692 aa）
Chain E 1–692（692 aa）
Chain F 1–692（692 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) 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) GOL GLYCEROL × 30 CU COPPER (II) ION × 6 PEO HYDROGEN PEROXIDE × 4 ABN BENZYLAMINE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；8% PEG8000, 0.22 M potassium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.25 Å R-free 0.230
4KFD Crystal structure of Hansenula polymorpha copper amine oxidase-1 reduced by methylamine at pH 6.0 Deposited 2013-04-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–692（692 aa）
Chain B 1–692（692 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 PEO HYDROGEN PEROXIDE × 2 GOL GLYCEROL × 20 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8.0-9.5% PEG8000, 0.28-0.30 M phosphate , pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.69 Å R-free 0.164
4KFD Crystal structure of Hansenula polymorpha copper amine oxidase-1 reduced by methylamine at pH 6.0 Deposited 2013-04-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 1–692（692 aa）
Chain D 1–692（692 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 PEO HYDROGEN PEROXIDE × 2 GOL GLYCEROL × 17 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8.0-9.5% PEG8000, 0.28-0.30 M phosphate , pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.69 Å R-free 0.164
4KFD Crystal structure of Hansenula polymorpha copper amine oxidase-1 reduced by methylamine at pH 6.0 Deposited 2013-04-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 1–692（692 aa）
Chain F 1–692（692 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 PEO HYDROGEN PEROXIDE × 2 GOL GLYCEROL × 15 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；298 K；8.0-9.5% PEG8000, 0.28-0.30 M phosphate , pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.69 Å R-free 0.164
4KFE Crystal structure of Hansenula polymorpha copper amine oxidase-1 reduced by methylamine at pH 7.0 Deposited 2013-04-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–692（692 aa）
Chain B 1–692（692 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 PEO HYDROGEN PEROXIDE × 2 FOR FORMYL GROUP × 2 GOL GLYCEROL × 22 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；8.0-9.5% PEG8000, 0.28-0.30 M phosphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.10 Å R-free 0.180
4KFE Crystal structure of Hansenula polymorpha copper amine oxidase-1 reduced by methylamine at pH 7.0 Deposited 2013-04-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 1–692（692 aa）
Chain D 1–692（692 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 PEO HYDROGEN PEROXIDE × 2 FOR FORMYL GROUP × 1 GOL GLYCEROL × 16 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；8.0-9.5% PEG8000, 0.28-0.30 M phosphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.10 Å R-free 0.180
4KFE Crystal structure of Hansenula polymorpha copper amine oxidase-1 reduced by methylamine at pH 7.0 Deposited 2013-04-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 1–692（692 aa）
Chain F 1–692（692 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 PEO HYDROGEN PEROXIDE × 2 GOL GLYCEROL × 14 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；8.0-9.5% PEG8000, 0.28-0.30 M phosphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.10 Å R-free 0.180
4KFF Crystal structure of Hansenula polymorpha copper amine oxidase-1 reduced by methylamine at pH 8.5 Deposited 2013-04-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–692（692 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 GOL GLYCEROL × 14 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；298 K；8.0-9.5% PEG8000, 0.28-0.30 M phosphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.15 Å R-free 0.185
4KFF Crystal structure of Hansenula polymorpha copper amine oxidase-1 reduced by methylamine at pH 8.5 Deposited 2013-04-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 1–692（692 aa）
Chain C 1–692（692 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 GOL GLYCEROL × 7 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；298 K；8.0-9.5% PEG8000, 0.28-0.30 M phosphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.15 Å R-free 0.185

14 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AMO_PICAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–655； UniProt 18–672 Author chain B； PDBConstruct 1–655； UniProt 18–672 Author chain C； PDBConstruct 1–655； UniProt 18–672 Author chain D； PDBConstruct 1–655； UniProt 18–672 Author chain E； PDBConstruct 1–655； UniProt 18–672 Author chain F； PDBConstruct 1–655； UniProt 18–672

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1a2v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a2v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a2v
Deposition date deposition_date1998-01-12
Structure title titleCOPPER AMINE OXIDASE FROM HANSENULA POLYMORPHA
Keywords keywordsAMINE OXIDASE, QUINOPROTEIN, TOPAQUINONE ENZYME, TPQ; AMINE OXIDASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier52.19 Å
Radius of gyration Rg (electron density) rg_electron51.71 Å
Forward intensity I(0) i02766160000.00
Molecular weight molecular_weight441910.0 kDa
Excluded volume excluded_volume551630 ų
Envelope volume envelope_volume723020 ų
Hydration-shell volume shell_volume108250 ų
Envelope diameter envelope_diameter154.5 Å
Shell Rg shell_rg63.20 Å
Envelope Rg envelope_rg50.21 Å
Shape Rg shape_rg51.68 Å
Total Rg total_rg52.11 Å
Total atoms total_atoms31170
Residues n_residues3924
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax139.7 Å
Rg (real space) rg_real51.93 Å
Rg uncertainty (real space) rg_real_error0.64 Å
I(0) (real space) i0_real2.7660e+09
I(0) uncertainty (real space) i0_real_error4.3830e+07
Rg (reciprocal space) rg_reciprocal52.38 Å
I(0) (reciprocal space) i0_reciprocal2768000000.0000
Solution quality estimate total_estimate0.8418
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary79.1 Å
Skewness Skewness skewness-0.025
Kurtosis Kurtosis kurtosis-0.812
Angular range angular_range— – 0.1500 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha970100000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 1.000; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (18 domains)

Domain ID domain_idd1a2va1
Class classb — All beta proteins
Fold Fold foldb.30 — Supersandwich
Superfamily Superfamily superfamilyb.30.2 — Amine oxidase catalytic domain
Family Family familyb.30.2.1 — Amine oxidase catalytic domain
Domain ID domain_idd1a2va2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd1a2va3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd1a2vb1
Class classb — All beta proteins
Fold Fold foldb.30 — Supersandwich
Superfamily Superfamily superfamilyb.30.2 — Amine oxidase catalytic domain
Family Family familyb.30.2.1 — Amine oxidase catalytic domain
Domain ID domain_idd1a2vb2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd1a2vb3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd1a2vc1
Class classb — All beta proteins
Fold Fold foldb.30 — Supersandwich
Superfamily Superfamily superfamilyb.30.2 — Amine oxidase catalytic domain
Family Family familyb.30.2.1 — Amine oxidase catalytic domain
Domain ID domain_idd1a2vc2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd1a2vc3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd1a2vd1
Class classb — All beta proteins
Fold Fold foldb.30 — Supersandwich
Superfamily Superfamily superfamilyb.30.2 — Amine oxidase catalytic domain
Family Family familyb.30.2.1 — Amine oxidase catalytic domain
Domain ID domain_idd1a2vd2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd1a2vd3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd1a2ve1
Class classb — All beta proteins
Fold Fold foldb.30 — Supersandwich
Superfamily Superfamily superfamilyb.30.2 — Amine oxidase catalytic domain
Family Family familyb.30.2.1 — Amine oxidase catalytic domain
Domain ID domain_idd1a2ve2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd1a2ve3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd1a2vf1
Class classb — All beta proteins
Fold Fold foldb.30 — Supersandwich
Superfamily Superfamily superfamilyb.30.2 — Amine oxidase catalytic domain
Family Family familyb.30.2.1 — Amine oxidase catalytic domain
Domain ID domain_idd1a2vf2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd1a2vf3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region

CATH v4.4 (18 domains)

Domain ID domain_id1a2vA01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40 —
Domain ID domain_id1a2vA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40 —
Domain ID domain_id1a2vA03
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily20 — Copper amine oxidase, catalytic domain
Domain ID domain_id1a2vB01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40 —
Domain ID domain_id1a2vB02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40 —
Domain ID domain_id1a2vB03
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily20 — Copper amine oxidase, catalytic domain
Domain ID domain_id1a2vC01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40 —
Domain ID domain_id1a2vC02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40 —
Domain ID domain_id1a2vC03
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily20 — Copper amine oxidase, catalytic domain
Domain ID domain_id1a2vD01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40 —
Domain ID domain_id1a2vD02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40 —
Domain ID domain_id1a2vD03
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily20 — Copper amine oxidase, catalytic domain
Domain ID domain_id1a2vE01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40 —
Domain ID domain_id1a2vE02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40 —
Domain ID domain_id1a2vE03
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily20 — Copper amine oxidase, catalytic domain
Domain ID domain_id1a2vF01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40 —
Domain ID domain_id1a2vF02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40 —
Domain ID domain_id1a2vF03
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily20 — Copper amine oxidase, catalytic domain
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8. Citations (1)

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9. Files and Curves (10)