2oov

Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms

Method: X-RAY DIFFRACTION

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

Peroxisomal copper amine oxidase

Pichia angusta

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	COPPER (II) ION × 2 GLYCEROL × 12 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	COPPER (II) ION × 2 GLYCEROL × 6 PHOSPHATE ION × 1 water × 2	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	COPPER (II) ION × 2 GLYCEROL × 10 PHOSPHATE ION × 1 water × 2	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 6	COPPER (II) ION × 6 GLYCEROL × 28 PHOSPHATE ION × 2 water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	AMO_PICAN
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–660； UniProt 13–672 Author chain B； PDBConstruct 1–660； UniProt 13–672 Author chain C； PDBConstruct 1–660； UniProt 13–672 Author chain D； PDBConstruct 1–660； UniProt 13–672 Author chain E； PDBConstruct 1–660； UniProt 13–672 Author chain F； PDBConstruct 1–660； UniProt 13–672

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2oov
Deposition date deposition_date	2007-01-26
Structure title title	Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms
Keywords keywords	protein-derived cofactor, beta-sandwich, TPQ, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

2oov__assembly_3__model_1

Assembly 3 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2oov__assembly_3__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2oov__assembly_3__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	32.93 Å
Rg (electron density)	32.21 Å
Total Rg	32.87 Å
Atom count	10455
Residues	1308
Excluded volume	185090 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2oov__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2oov__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2oov__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`2oov__assembly_4__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Peroxisomal copper amine oxidase
Molecular weight formula_weight	74077.4 kDa
EC 编号 ec_number	1.4.3.6
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	36770

AASAAPARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLREPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLVDLASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIEQCVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVYYRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSKHKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGNVMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRISLSEMIVPYGSPEFPHQRKHALDIGEYGAGYMTNPLSLGCDCKGVIHYLDAHFSDRAGDPITVKNAVCIHEEDDGLLFKHSDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQDGAIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQHLFSLRIDPRIDGDGNSAAACDAKSSPYPLGSPENMYGNAFYSEKTTFKTVKDSLTNYESATGRSWDIFNPNKVNPYSGKPPSYKLVSTQCPPLLAKEGSLVAKRAPWASHSVNVVPYKDNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILFFHTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDIQPSYAMTTSEAKRAV

Source Source

Source organism organism	Pichia angusta
NCBI taxonomy ID ncbi_taxonomy_id	4905
Host organism host_organism	Saccharomyces cerevisiae

Entity 2 Entity 2 polymer

Description description	Peroxisomal copper amine oxidase
Molecular weight formula_weight	74061.4 kDa
EC 编号 ec_number	1.4.3.6
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D,E,F

Source Source

Source organism organism	Pichia angusta
NCBI taxonomy ID ncbi_taxonomy_id	4905
Host organism host_organism	Saccharomyces cerevisiae

Entity 3 Entity 3 non-polymer

Description description	COPPER (II) ION
Molecular weight formula_weight	63.5 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	28

Entity 5 Entity 5 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	5055

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6. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (18 domains)

Domain ID domain_id	d2oova1
Class class	b — All beta proteins
Fold Fold fold	b.30 — Supersandwich
Superfamily Superfamily superfamily	b.30.2 — Amine oxidase catalytic domain
Family Family family	b.30.2.1 — Amine oxidase catalytic domain

Domain ID domain_id	d2oova2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d2oova3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d2oovb1
Class class	b — All beta proteins
Fold Fold fold	b.30 — Supersandwich
Superfamily Superfamily superfamily	b.30.2 — Amine oxidase catalytic domain
Family Family family	b.30.2.1 — Amine oxidase catalytic domain

Domain ID domain_id	d2oovb2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d2oovb3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d2oovc1
Class class	b — All beta proteins
Fold Fold fold	b.30 — Supersandwich
Superfamily Superfamily superfamily	b.30.2 — Amine oxidase catalytic domain
Family Family family	b.30.2.1 — Amine oxidase catalytic domain

Domain ID domain_id	d2oovc2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d2oovc3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d2oovd1
Class class	b — All beta proteins
Fold Fold fold	b.30 — Supersandwich
Superfamily Superfamily superfamily	b.30.2 — Amine oxidase catalytic domain
Family Family family	b.30.2.1 — Amine oxidase catalytic domain

Domain ID domain_id	d2oovd2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d2oovd3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d2oove1
Class class	b — All beta proteins
Fold Fold fold	b.30 — Supersandwich
Superfamily Superfamily superfamily	b.30.2 — Amine oxidase catalytic domain
Family Family family	b.30.2.1 — Amine oxidase catalytic domain

Domain ID domain_id	d2oove2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d2oove3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d2oovf1
Class class	b — All beta proteins
Fold Fold fold	b.30 — Supersandwich
Superfamily Superfamily superfamily	b.30.2 — Amine oxidase catalytic domain
Family Family family	b.30.2.1 — Amine oxidase catalytic domain

Domain ID domain_id	d2oovf2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d2oovf3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

CATH v4.4 (18 domains)

Domain ID domain_id	2oovA01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	2oovA02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	2oovA03
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily	20 — Copper amine oxidase, catalytic domain

Domain ID domain_id	2oovB01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	2oovB02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	2oovB03
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily	20 — Copper amine oxidase, catalytic domain

Domain ID domain_id	2oovC01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	2oovC02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	2oovC03
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily	20 — Copper amine oxidase, catalytic domain

Domain ID domain_id	2oovD01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	2oovD02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	2oovD03
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily	20 — Copper amine oxidase, catalytic domain

Domain ID domain_id	2oovE01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	2oovE02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	2oovE03
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily	20 — Copper amine oxidase, catalytic domain

Domain ID domain_id	2oovF01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	2oovF02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	2oovF03
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily	20 — Copper amine oxidase, catalytic domain

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Unit-cell length a length_a	104.146 Å
Unit-cell length b length_b	223.082 Å
Unit-cell length c length_c	104.248 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	95.77 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.700 Å
Low-resolution limit resolution_low	37.960 Å
R factor r_factor	0.1490
R_work r_work	0.1470
R_free r_free	0.1780

Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms

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

Peroxisomal copper amine oxidase

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2oov__assembly_3__model_1

2oov__assembly_3__model_1 | I(q)

2oov__assembly_3__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (18 domains)

CATH v4.4 (18 domains)

7. Citations (1)

Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms

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

Peroxisomal copper amine oxidase

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2oov__assembly_3__model_1

2oov__assembly_3__model_1 | I(q)

2oov__assembly_3__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (18 domains)

CATH v4.4 (18 domains)

7. Citations (1)