2vvl

The structure of MAO-N-D3, a variant of monoamine oxidase from Aspergillus niger.

Method: X-RAY DIFFRACTION

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

MONOAMINE OXIDASE N

ASPERGILLUS NIGER

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	FLAVIN-ADENINE DINUCLEOTIDE × 2 1,2-ETHANEDIOL × 1 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	FLAVIN-ADENINE DINUCLEOTIDE × 2 1,2-ETHANEDIOL × 2 water × 2	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	FLAVIN-ADENINE DINUCLEOTIDE × 2 1,2-ETHANEDIOL × 1 water × 2	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 2	FLAVIN-ADENINE DINUCLEOTIDE × 2 1,2-ETHANEDIOL × 3 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	AOFN_ASPNG
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–495； UniProt 1–495 Author chain B； PDBConstruct 1–495； UniProt 1–495 Author chain C； PDBConstruct 1–495； UniProt 1–495 Author chain D； PDBConstruct 1–495； UniProt 1–495 Author chain E； PDBConstruct 1–495； UniProt 1–495 Author chain F； PDBConstruct 1–495； UniProt 1–495 Author chain H； PDBConstruct 1–495； UniProt 1–495 Author chain G； PDBConstruct 1–495； UniProt 1–495

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	2vvl
Deposition date deposition_date	2008-06-10
Structure title title	The structure of MAO-N-D3, a variant of monoamine oxidase from Aspergillus niger.
Keywords keywords	MONOAMINE OXIDASE, ASPERGILLUS NIGER, FAD, PEROXISOME, FLAVOPROTEIN, OXIDOREDUCTASE, ENANTIOSELECTIVITY, DIRECTED EVOLUTION VARIANT; 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.

2vvl__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2vvl__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2vvl__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	29.21 Å
Rg (electron density)	28.30 Å
Total Rg	29.17 Å
Atom count	7646
Residues	953
Excluded volume	134220 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2vvl__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2vvl__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2vvl__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`2vvl__assembly_4__model_1`	dimeric （2）	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 (5)

Entity 1 Entity 1 polymer

Description description	MONOAMINE OXIDASE N
Molecular weight formula_weight	55590.5 kDa
EC 编号 ec_number	1.4.3.4
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	7

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,H
Atom count atom_count	31496

MTSRDGYQWTPETGLTQGVPSLGVISPPTNIEDTDKDGPWDVIVIGGGYCGLTATRDLTVAGFKTLLLEARDRIGGRSWSSNIDGYPYEMGGTWVHWHQSHVWREITRYKMHNALSPSFNFSRGVNHFQLRTNPTTSTYMTHEAEDELLRSALHKFTNVDGTNGRTVLPFPHDMFYVPEFRKYDEMSYSERIDQIRDELSLNERSSLEAFILLCSGGTLENSSFGEFLHWWAMSGYTYQGCMDCLMSYKFKDGQSAFARRFWEEAAGTGRLGYVFGCPVRSVVNERDAARVTARDGREFVAKRVVCTIPLNVLSTIQFSPALSTERISAMQAGHVSMCTKVHAEVDNKDMRSWTGIAYPFNKLCYAIGDGTTPAGNTHLVCFGTDANHIQPDEDVRETLKAVGQLAPGTFGVKRLVFHNWVKDEFAKGAWFFSRPGMVSECLQGLREKHGGVVFANSDWALGWRSFIDGAIEEGTRAARVVLEELGTKREVKARL

Source Source

Source organism organism	ASPERGILLUS NIGER
NCBI taxonomy ID ncbi_taxonomy_id	5061
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	MONOAMINE OXIDASE N
Molecular weight formula_weight	55594.4 kDa
EC 编号 ec_number	1.4.3.4
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G

MTSRDGYQWTPETGLTQGVTSLGVISPPTNIEDTDKDGPWDVIVIGGGYCGLTATRDLTVAGFKTLLLEARDRIGGRSWSSNIDGYPYEMGGTWVHWHQSHVWREITRYKMHNALSPSFNFSRGVNHFQLRTNPTTSTYMTHEAEDELLRSALHKFTNVDGTNGRTVLPFPHDMFYVPEFRKYDEMSYSERIDQIRDELSLNERSSLEAFILLCSGGTLENSSFGEFLHWWAMSGYTYQGCMDCLMSYKFKDGQSAFARRFWEEAAGTGRLGYVFGCPVRSVVNERDAARVTARDGREFVAKRVVCTIPLNVLSTIQFSPALSTERISAMQAGHVSMCTKVHAEVDNKDMRSWTGIAYPFNKLCYAIGDGTTPAGNTHLVCFGTDANHIQPDEDVRETLKAVGQLAPGTFGVKRLVFHNWVKDEFAKGAWFFSRPGMVSECLQGLREKHGGVVFANSDWALGWRSFIDGAIEEGTRAARVVLEELGTKREVKARL

Source Source

Source organism organism	ASPERGILLUS NIGER
NCBI taxonomy ID ncbi_taxonomy_id	5061
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 non-polymer

Description description	FLAVIN-ADENINE DINUCLEOTIDE
Molecular weight formula_weight	785.5 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 4 Entity 4 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	807

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6. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

Domain ID domain_id	2vvlA01
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	2vvlA02
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	2vvlB01
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	2vvlB02
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	2vvlC01
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	2vvlC02
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	2vvlD01
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	2vvlD02
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	2vvlE01
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	2vvlE02
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	2vvlF01
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	2vvlF02
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	2vvlG01
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	2vvlG02
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	2vvlH01
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	2vvlH02
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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Unit-cell length a length_a	103.287 Å
Unit-cell length b length_b	187.248 Å
Unit-cell length c length_c	132.432 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.10 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	14

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

Resolution resolution	2.450 Å
Low-resolution limit resolution_low	132.450 Å
R factor r_factor	0.1850
R_work r_work	0.1820
R_free r_free	0.2360

The structure of MAO-N-D3, a variant of monoamine oxidase from Aspergillus niger.

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

MONOAMINE OXIDASE N

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

2vvl__assembly_2__model_1

2vvl__assembly_2__model_1 | I(q)

2vvl__assembly_2__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 (5)

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 water

6. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

7. Citations (1)

The structure of MAO-N-D3, a variant of monoamine oxidase from Aspergillus niger.

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

MONOAMINE OXIDASE N

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

2vvl__assembly_2__model_1

2vvl__assembly_2__model_1 | I(q)

2vvl__assembly_2__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 (5)

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 water

6. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

7. Citations (1)