2c12

Crystal Structure of Nitroalkane Oxidase in Complex with Spermine, a Competitive Inhibitor

Method: X-RAY DIFFRACTION

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

NITROALKANE OXIDASE

FUSARIUM OXYSPORUM

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	FLAVIN-ADENINE DINUCLEOTIDE × 4 GLYCEROL × 11 SPERMINE × 3 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 water × 4	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 4	FLAVIN-ADENINE DINUCLEOTIDE × 4 GLYCEROL × 8 SPERMINE × 2 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q8X1D8_FUSOX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–439； UniProt 1–439 Author chain B； PDBConstruct 1–439； UniProt 1–439 Author chain C； PDBConstruct 1–439； UniProt 1–439 Author chain D； PDBConstruct 1–439； UniProt 1–439 Author chain E； PDBConstruct 1–439； UniProt 1–439 Author chain F； PDBConstruct 1–439； UniProt 1–439

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	2c12
Deposition date deposition_date	2005-09-10
Structure title title	Crystal Structure of Nitroalkane Oxidase in Complex with Spermine, a Competitive Inhibitor
Keywords keywords	OXIDOREDUCTASE, FLAVOENZYME, NITROALKANE, ACYL-COA DEHYDROGENASE, LONG CELL EDGE, FAD, INHIBITOR, FLAVOPROTEIN; 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.

2c12__assembly_1__model_1

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

Download this curve (.dat)

2c12__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2c12__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	35.56 Å
Rg (electron density)	34.76 Å
Total Rg	35.16 Å
Atom count	13572
Residues	1720
Excluded volume	242270 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2c12__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2c12__assembly_2__model_1`	tetrameric （4）	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	NITROALKANE OXIDASE
Molecular weight formula_weight	48219.2 kDa
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	21487

MVDFKLSPSQLEARRHAQAFANTVLTKASAEYSTQKDQLSRFQATRPFYREAVRHGLIKAQVPIPLGGTMESLVHESIILEELFAVEPATSITIVATALGLMPVILCDSPSLQEKFLKPFISGEGEPLASLMHSEPNGTANWLQKGGPGLQTTARKVGNEWVISGEKLWPSNSGGWDYKGADLACVVCRVSDDPSKPQDPNVDPATQIAVLLVTRETIANNKKDAYQILGEPELAGHITTSGPHTRFTEFHVPHENLLCTPGLKAQGLVETAFAMSAALVGAMAIGTARAAFEEALVFAKSDTRGGSKHIIEHQSVADKLIDCKIRLETSRLLVWKAVTTLEDEALEWKVKLEMAMQTKIYTTDVAVECVIDAMKAVGMKSYAKDMSFPRLLNEVMCYPLFDGGNIGLRRRQMQRVMALEDYEPWAATYGSSKVDKSRL

Source Source

Source organism organism	FUSARIUM OXYSPORUM
NCBI taxonomy ID ncbi_taxonomy_id	5507
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	FLAVIN-ADENINE DINUCLEOTIDE
Molecular weight formula_weight	785.5 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 3 Entity 3 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	15

Entity 4 Entity 4 non-polymer

Description description	SPERMINE
Molecular weight formula_weight	202.3 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 5 Entity 5 non-polymer

Description description	2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
Molecular weight formula_weight	354.4 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	1117

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6. Fold Classification (SCOP + CATH) 30 domains

SCOP 2.08 (12 domains)

Domain ID domain_id	d2c12a1
Class class	a — All alpha proteins
Fold Fold fold	a.29 — Bromodomain-like
Superfamily Superfamily superfamily	a.29.3 — Acyl-CoA dehydrogenase C-terminal domain-like
Family Family family	a.29.3.1 — Medium chain acyl-CoA dehydrogenase-like, C-terminal domain

Domain ID domain_id	d2c12a2
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.6 — Acyl-CoA dehydrogenase NM domain-like
Superfamily Superfamily superfamily	e.6.1 — Acyl-CoA dehydrogenase NM domain-like
Family Family family	e.6.1.1 — Medium chain acyl-CoA dehydrogenase, NM (N-terminal and middle) domains

Domain ID domain_id	d2c12b1
Class class	a — All alpha proteins
Fold Fold fold	a.29 — Bromodomain-like
Superfamily Superfamily superfamily	a.29.3 — Acyl-CoA dehydrogenase C-terminal domain-like
Family Family family	a.29.3.1 — Medium chain acyl-CoA dehydrogenase-like, C-terminal domain

Domain ID domain_id	d2c12b2
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.6 — Acyl-CoA dehydrogenase NM domain-like
Superfamily Superfamily superfamily	e.6.1 — Acyl-CoA dehydrogenase NM domain-like
Family Family family	e.6.1.1 — Medium chain acyl-CoA dehydrogenase, NM (N-terminal and middle) domains

Domain ID domain_id	d2c12c1
Class class	a — All alpha proteins
Fold Fold fold	a.29 — Bromodomain-like
Superfamily Superfamily superfamily	a.29.3 — Acyl-CoA dehydrogenase C-terminal domain-like
Family Family family	a.29.3.1 — Medium chain acyl-CoA dehydrogenase-like, C-terminal domain

Domain ID domain_id	d2c12c2
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.6 — Acyl-CoA dehydrogenase NM domain-like
Superfamily Superfamily superfamily	e.6.1 — Acyl-CoA dehydrogenase NM domain-like
Family Family family	e.6.1.1 — Medium chain acyl-CoA dehydrogenase, NM (N-terminal and middle) domains

Domain ID domain_id	d2c12d1
Class class	a — All alpha proteins
Fold Fold fold	a.29 — Bromodomain-like
Superfamily Superfamily superfamily	a.29.3 — Acyl-CoA dehydrogenase C-terminal domain-like
Family Family family	a.29.3.1 — Medium chain acyl-CoA dehydrogenase-like, C-terminal domain

Domain ID domain_id	d2c12d2
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.6 — Acyl-CoA dehydrogenase NM domain-like
Superfamily Superfamily superfamily	e.6.1 — Acyl-CoA dehydrogenase NM domain-like
Family Family family	e.6.1.1 — Medium chain acyl-CoA dehydrogenase, NM (N-terminal and middle) domains

Domain ID domain_id	d2c12e1
Class class	a — All alpha proteins
Fold Fold fold	a.29 — Bromodomain-like
Superfamily Superfamily superfamily	a.29.3 — Acyl-CoA dehydrogenase C-terminal domain-like
Family Family family	a.29.3.1 — Medium chain acyl-CoA dehydrogenase-like, C-terminal domain

Domain ID domain_id	d2c12e2
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.6 — Acyl-CoA dehydrogenase NM domain-like
Superfamily Superfamily superfamily	e.6.1 — Acyl-CoA dehydrogenase NM domain-like
Family Family family	e.6.1.1 — Medium chain acyl-CoA dehydrogenase, NM (N-terminal and middle) domains

Domain ID domain_id	d2c12f1
Class class	a — All alpha proteins
Fold Fold fold	a.29 — Bromodomain-like
Superfamily Superfamily superfamily	a.29.3 — Acyl-CoA dehydrogenase C-terminal domain-like
Family Family family	a.29.3.1 — Medium chain acyl-CoA dehydrogenase-like, C-terminal domain

Domain ID domain_id	d2c12f2
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.6 — Acyl-CoA dehydrogenase NM domain-like
Superfamily Superfamily superfamily	e.6.1 — Acyl-CoA dehydrogenase NM domain-like
Family Family family	e.6.1.1 — Medium chain acyl-CoA dehydrogenase, NM (N-terminal and middle) domains

CATH v4.4 (18 domains)

Domain ID domain_id	2c12A01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	540 — Butyryl-Coa Dehydrogenase, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acyl-CoA dehydrogenase/oxidase, N-terminal domain

Domain ID domain_id	2c12A02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	110 — Butyryl-CoA Dehydrogenase, subunit A; domain 2
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 2

Domain ID domain_id	2c12A03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 3

Domain ID domain_id	2c12B01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	540 — Butyryl-Coa Dehydrogenase, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acyl-CoA dehydrogenase/oxidase, N-terminal domain

Domain ID domain_id	2c12B02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	110 — Butyryl-CoA Dehydrogenase, subunit A; domain 2
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 2

Domain ID domain_id	2c12B03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 3

Domain ID domain_id	2c12C01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	540 — Butyryl-Coa Dehydrogenase, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acyl-CoA dehydrogenase/oxidase, N-terminal domain

Domain ID domain_id	2c12C02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	110 — Butyryl-CoA Dehydrogenase, subunit A; domain 2
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 2

Domain ID domain_id	2c12C03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 3

Domain ID domain_id	2c12D01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	540 — Butyryl-Coa Dehydrogenase, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acyl-CoA dehydrogenase/oxidase, N-terminal domain

Domain ID domain_id	2c12D02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	110 — Butyryl-CoA Dehydrogenase, subunit A; domain 2
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 2

Domain ID domain_id	2c12D03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 3

Domain ID domain_id	2c12E01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	540 — Butyryl-Coa Dehydrogenase, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acyl-CoA dehydrogenase/oxidase, N-terminal domain

Domain ID domain_id	2c12E02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	110 — Butyryl-CoA Dehydrogenase, subunit A; domain 2
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 2

Domain ID domain_id	2c12E03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 3

Domain ID domain_id	2c12F01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	540 — Butyryl-Coa Dehydrogenase, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acyl-CoA dehydrogenase/oxidase, N-terminal domain

Domain ID domain_id	2c12F02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	110 — Butyryl-CoA Dehydrogenase, subunit A; domain 2
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 2

Domain ID domain_id	2c12F03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 3

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Unit-cell length a length_a	103.393 Å
Unit-cell length b length_b	103.393 Å
Unit-cell length c length_c	485.134 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 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	2.070 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.1900
R_work r_work	0.1880
R_free r_free	0.2250

Crystal Structure of Nitroalkane Oxidase in Complex with Spermine, a Competitive Inhibitor

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

NITROALKANE 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

2c12__assembly_1__model_1

2c12__assembly_1__model_1 | I(q)

2c12__assembly_1__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 non-polymer

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) 30 domains

SCOP 2.08 (12 domains)

CATH v4.4 (18 domains)

7. Citations (3)

Crystal Structure of Nitroalkane Oxidase in Complex with Spermine, a Competitive Inhibitor

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

NITROALKANE 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

2c12__assembly_1__model_1

2c12__assembly_1__model_1 | I(q)

2c12__assembly_1__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 non-polymer

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) 30 domains

SCOP 2.08 (12 domains)

CATH v4.4 (18 domains)

7. Citations (3)