SAXSdb — 1h82

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1. Protein Identity and Related Structures Protein Identity & Related Structures

POLYAMINE OXIDASE

OrganismNot specified

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 29–500 Chain B； UniProt 29–500	Fragment：FAD-BINDING DOMAIN RESIDUES 29-500	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GZZ N-{8-[(8-{[(E)-AMINO(IMINO)METHYL]AMINO}OCTYL)AMINO]OCTYL}GUANIDINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 4.6；pH 4.60	Resolution 1.90 Å R-free 0.231
2	Other combination Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 29–500	Fragment：FAD-BINDING DOMAIN RESIDUES 29-500	;alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-D-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GZZ N-{8-[(8-{[(E)-AMINO(IMINO)METHYL]AMINO}OCTYL)AMINO]OCTYL}GUANIDINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 4.6；pH 4.60	Resolution 1.90 Å R-free 0.231

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 1H82	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B37 A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE Deposited 1998-12-17	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 29–500（472 aa） Fragment：FAD-BINDING DOMAIN	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.6	Resolution 1.90 Å
1B37 A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE Deposited 1998-12-17	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain B 29–500（472 aa） Fragment：FAD-BINDING DOMAIN	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.6	Resolution 1.90 Å
1B37 A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE Deposited 1998-12-17	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain C 29–500（472 aa） Fragment：FAD-BINDING DOMAIN	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.6	Resolution 1.90 Å
1B37 A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE Deposited 1998-12-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Other combination Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 29–500（472 aa） Fragment：FAD-BINDING DOMAIN Chain B 29–500（472 aa） Fragment：FAD-BINDING DOMAIN Chain C 29–500（472 aa） Fragment：FAD-BINDING DOMAIN	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.6	Resolution 1.90 Å
1B37 A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE Deposited 1998-12-17	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 29–500（472 aa） Fragment：FAD-BINDING DOMAIN Chain B 29–500（472 aa） Fragment：FAD-BINDING DOMAIN	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.6	Resolution 1.90 Å
1B37 A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE Deposited 1998-12-17	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 29–500（472 aa） Fragment：FAD-BINDING DOMAIN	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.6	Resolution 1.90 Å
1H81 STRUCTURE OF POLYAMINE OXIDASE IN THE REDUCED STATE Deposited 2001-01-24	Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 29–500（472 aa） Fragment：FAD-BINDING DOMAIN RESIDUES 29-500 Chain B 29–500（472 aa） Fragment：FAD-BINDING DOMAIN RESIDUES 29-500	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.60	Resolution 2.10 Å R-free 0.235
1H81 STRUCTURE OF POLYAMINE OXIDASE IN THE REDUCED STATE Deposited 2001-01-24	Different ligand/ion Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 29–500（472 aa） Fragment：FAD-BINDING DOMAIN RESIDUES 29-500	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.60	Resolution 2.10 Å R-free 0.235
1H83 STRUCTURE OF POLYAMINE OXIDASE IN COMPLEX WITH 1,8-DIAMINOOCTANE Deposited 2001-01-24	Different construct Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 29–500（472 aa） Fragment：FAD-BINDING DOMAIN Chain B 29–500（472 aa） Fragment：FAD-BINDING DOMAIN	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 DIA OCTANE 1,8-DIAMINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.60	Resolution 1.90 Å R-free 0.237
1H83 STRUCTURE OF POLYAMINE OXIDASE IN COMPLEX WITH 1,8-DIAMINOOCTANE Deposited 2001-01-24	Different construct Different ligand/ion Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 29–500（472 aa） Fragment：FAD-BINDING DOMAIN	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 DIA OCTANE 1,8-DIAMINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.60	Resolution 1.90 Å R-free 0.237
1H84 COVALENT ADDUCT BETWEEN POLYAMINE OXIDASE AND N1ethylN11((cycloheptyl)methyl)4,8diazaundecane at pH 4.6 Deposited 2001-01-24	Different construct Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 29–500（472 aa） Fragment：FAD-BINDING DOMAIN Chain B 29–500（472 aa） Fragment：FAD-BINDING DOMAIN	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NBA 3-[(3-{[3-(METHYLAMINO)PROPYL]AMINO}PROPYL)AMINO]PROPANE-1,1-DIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.60	Resolution 2.00 Å R-free 0.227
1H84 COVALENT ADDUCT BETWEEN POLYAMINE OXIDASE AND N1ethylN11((cycloheptyl)methyl)4,8diazaundecane at pH 4.6 Deposited 2001-01-24	Different construct Different ligand/ion Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 29–500（472 aa） Fragment：FAD-BINDING DOMAIN	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NBA 3-[(3-{[3-(METHYLAMINO)PROPYL]AMINO}PROPYL)AMINO]PROPANE-1,1-DIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.60	Resolution 2.00 Å R-free 0.227
1H86 COVALENT ADDUCT BETWEEN POLYAMINE OXIDASE AND N1ethylN11((cycloheptyl)methyl)4,8diazaundecane at pH 7.0 Deposited 2001-01-24	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 29–500（472 aa） Chain B 29–500（472 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NBA 3-[(3-{[3-(METHYLAMINO)PROPYL]AMINO}PROPYL)AMINO]PROPANE-1,1-DIOL × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7.00	Resolution 2.00 Å R-free 0.229
1H86 COVALENT ADDUCT BETWEEN POLYAMINE OXIDASE AND N1ethylN11((cycloheptyl)methyl)4,8diazaundecane at pH 7.0 Deposited 2001-01-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 29–500（472 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NBA 3-[(3-{[3-(METHYLAMINO)PROPYL]AMINO}PROPYL)AMINO]PROPANE-1,1-DIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7.00	Resolution 2.00 Å R-free 0.229
3KPF X-ray structure of the mutant Lys300Met of polyamine oxidase from Zea mays Deposited 2009-11-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 29–500（472 aa）	Mutation：K300M	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CL CHLORIDE ION × 1 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；293 K；50% SATURATED AMMONIUM SULFATE SOLUTION, 0.1M SODIUM ACETATE pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.90 Å R-free 0.223
3KPF X-ray structure of the mutant Lys300Met of polyamine oxidase from Zea mays Deposited 2009-11-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain B 29–500（472 aa）	Mutation：K300M	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 ACT ACETATE ION × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；293 K；50% SATURATED AMMONIUM SULFATE SOLUTION, 0.1M SODIUM ACETATE pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.90 Å R-free 0.223
3KPF X-ray structure of the mutant Lys300Met of polyamine oxidase from Zea mays Deposited 2009-11-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 29–500（472 aa） Chain B 29–500（472 aa）	Mutation：K300M Mutation：K300M	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CL CHLORIDE ION × 1 ACT ACETATE ION × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；293 K；50% SATURATED AMMONIUM SULFATE SOLUTION, 0.1M SODIUM ACETATE pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.90 Å R-free 0.223
3KU9 X-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermine Deposited 2009-11-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 29–500（472 aa）	Mutation：K300M	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SPM SPERMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；293 K；50% SATURATED AMMONIUM SULFATE SOLUTION, 0.1M SODIUM ACETATE PH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.20 Å R-free 0.219
3KU9 X-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermine Deposited 2009-11-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain B 29–500（472 aa）	Mutation：K300M	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SPM SPERMINE × 1 CL CHLORIDE ION × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；293 K；50% SATURATED AMMONIUM SULFATE SOLUTION, 0.1M SODIUM ACETATE PH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.20 Å R-free 0.219
3KU9 X-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermine Deposited 2009-11-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 29–500（472 aa） Chain B 29–500（472 aa）	Mutation：K300M Mutation：K300M	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SPM SPERMINE × 2 CL CHLORIDE ION × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；293 K；50% SATURATED AMMONIUM SULFATE SOLUTION, 0.1M SODIUM ACETATE PH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.20 Å R-free 0.219
3L1R X-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermidine Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 29–500（472 aa）	Mutation：K300M	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SPD SPERMIDINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；50% SATURATED AMMONIUM SULFATE SOLUTION, 0.1M SODIUM ACETATE PH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.20 Å R-free 0.216
3L1R X-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermidine Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain B 29–500（472 aa）	Mutation：K300M	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SPD SPERMIDINE × 1 SO4 SULFATE ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；50% SATURATED AMMONIUM SULFATE SOLUTION, 0.1M SODIUM ACETATE PH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.20 Å R-free 0.216
3L1R X-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermidine Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 29–500（472 aa） Chain B 29–500（472 aa）	Mutation：K300M Mutation：K300M	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SPD SPERMIDINE × 2 SO4 SULFATE ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；50% SATURATED AMMONIUM SULFATE SOLUTION, 0.1M SODIUM ACETATE PH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.20 Å R-free 0.216

8 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PAO_MAIZE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–472； UniProt 29–500 Author chain B； PDBConstruct 1–472； UniProt 29–500 Author chain C； PDBConstruct 1–472； UniProt 29–500

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1h82
Deposition date deposition_date	2001-01-24
Structure title title	STRUCTURE OF POLYAMINE OXIDASE IN COMPLEX WITH GUAZATINE
Keywords keywords	FLAVIN-DEPENDENT AMINE OXIDASE, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	42.84 Å
Radius of gyration Rg (electron density) rg_electron	42.63 Å
Forward intensity I(0) i0	387651000.00
Molecular weight molecular_weight	162470.0 kDa
Excluded volume excluded_volume	203310 Å³
Envelope volume envelope_volume	269970 Å³
Hydration-shell volume shell_volume	52872 Å³
Envelope diameter envelope_diameter	139.5 Å
Shell Rg shell_rg	47.60 Å
Envelope Rg envelope_rg	41.85 Å
Shape Rg shape_rg	42.57 Å
Total Rg total_rg	43.07 Å
Total atoms total_atoms	11464
Residues n_residues	1383
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	138.2 Å
Rg (real space) rg_real	42.87 Å
Rg uncertainty (real space) rg_real_error	1.21 Å
I(0) (real space) i0_real	3.8770e+08
I(0) uncertainty (real space) i0_real_error	7.0560e+06
Rg (reciprocal space) rg_reciprocal	42.84 Å
I(0) (reciprocal space) i0_reciprocal	387600000.0000
Solution quality estimate total_estimate	0.8715
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	33.6 Å
Skewness Skewness skewness	0.184
Kurtosis Kurtosis kurtosis	-0.887
Angular range angular_range	— – 0.1850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	110100000.0000
Real-space data points n_real_points	38
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.926; Smooth: 0.928

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	POLYAMINE OXIDASE
Molecular weight formula_weight	53698.5 kDa
EC 编号 ec_number	1.5.3.11
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	12210

ATVGPRVIVVGAGMSGISAAKRLSEAGITDLLILEATDHIGGRMHKTNFAGINVELGANWVEGVNGGKMNPIWPIVNSTLKLRNFRSDFDYLAQNVYKEDGGVYDEDYVQKRIELADSVEEMGEKLSATLHASGRDDMSILAMQRLNEHQPNGPATPVDMVVDYYKFDYEFAEPPRVTSLQNTVPLATFSDFGDDVYFVADQRGYEAVVYYLAGQYLKTDDKSGKIVDPRLQLNKVVREIKYSPGGVTVKTEDNSVYSADYVMVSASLGVLQSDLIQFKPKLPTWKVRAIYQFDMAVYTKIFLKFPRKFWPEGKGREFFLYASSRRGYYGVWQEFEKQYPDANVLLVTVTDEESRRIEQQSDEQTKAEIMQVLRKMFPGKDVPDATDILVPRWWSDRFYKGTFSNWPVGVNRYEYDQLRAPVGRVYFTGEHTSEHYNGYVHGAYLSGIDSAEILINCAQKKMCKYHVQGKYD

Entity 2 Entity 2 branched

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	424.4 kDa
Source method src_method	man
Copy count entity_count	2

Entity 3 Entity 3 branched

Description description	;alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-D-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	894.8 kDa
Source method src_method	man
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	FLAVIN-ADENINE DINUCLEOTIDE
Molecular weight formula_weight	785.5 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 5 Entity 5 non-polymer

Description description	N-{8-[(8-{[(E)-AMINO(IMINO)METHYL]AMINO}OCTYL)AMINO]OCTYL}GUANIDINE
Molecular weight formula_weight	355.6 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	746

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1h82a1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamily	c.3.1 — FAD/NAD(P)-binding domain
Family Family family	c.3.1.2 — FAD-linked reductases, N-terminal domain

Domain ID domain_id	d1h82a2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.16 — FAD-linked reductases, C-terminal domain
Superfamily Superfamily superfamily	d.16.1 — FAD-linked reductases, C-terminal domain
Family Family family	d.16.1.5 — L-aminoacid/polyamine oxidase

Domain ID domain_id	d1h82b1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamily	c.3.1 — FAD/NAD(P)-binding domain
Family Family family	c.3.1.2 — FAD-linked reductases, N-terminal domain

Domain ID domain_id	d1h82b2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.16 — FAD-linked reductases, C-terminal domain
Superfamily Superfamily superfamily	d.16.1 — FAD-linked reductases, C-terminal domain
Family Family family	d.16.1.5 — L-aminoacid/polyamine oxidase

Domain ID domain_id	d1h82c1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamily	c.3.1 — FAD/NAD(P)-binding domain
Family Family family	c.3.1.2 — FAD-linked reductases, N-terminal domain

Domain ID domain_id	d1h82c2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.16 — FAD-linked reductases, C-terminal domain
Superfamily Superfamily superfamily	d.16.1 — FAD-linked reductases, C-terminal domain
Family Family family	d.16.1.5 — L-aminoacid/polyamine oxidase

CATH v4.4 (6 domains)

Domain ID domain_id	1h82A01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	1h82A02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	660 — Polyamine Oxidase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1h82B01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	1h82B02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	660 — Polyamine Oxidase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1h82C01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	1h82C02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	660 — Polyamine Oxidase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 —

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8. Citations (1)

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Unit-cell length a length_a	184.970 Å
Unit-cell length b length_b	184.970 Å
Unit-cell length c length_c	282.240 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	36

Space group space_group	P 65 2 2
Space-group number int_tables_number	179
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.1990
R_work r_work	0.1990
R_free r_free	0.2310

fit	/app/data/saxs_computation/h8/1h82/1h82.fit
pddf	/app/data/pr_computation/h8/1h82/1h82.pr.out
profile	/app/data/saxs_computation/h8/1h82/1h82.dat

STRUCTURE OF POLYAMINE OXIDASE IN COMPLEX WITH GUAZATINE

1. Protein Identity and Related Structures Protein Identity & Related Structures

POLYAMINE OXIDASE

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction