SAXSdb — 2hkr

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

Aromatic amine dehydrogenase, small subunit

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Aromatic amine dehydrogenase, large subunit × 2 （Q0VKG7） 2-(4-METHOXYPHENYL)ETHANAMINE × 1 2-(4-METHOXYPHENYL)ACETAMIDE × 1 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q0VKG6_ALCFA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain D； PDBConstruct 1–122； UniProt 59–180 Author chain H； PDBConstruct 1–122； UniProt 59–180

Aromatic amine dehydrogenase, large subunit

Alcaligenes faecalis

UniProt Q0VKG7

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Aromatic amine dehydrogenase, small subunit × 2 （Q0VKG6） 2-(4-METHOXYPHENYL)ETHANAMINE × 1 2-(4-METHOXYPHENYL)ACETAMIDE × 1 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q0VKG7_ALCFA
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A； PDBConstruct 1–361； UniProt 4–364 Author chain B； PDBConstruct 1–361； UniProt 4–364

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	2hkr
Deposition date deposition_date	2006-07-05
Structure title title	Structures of the carbinolamine and schiff-base intermediates in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with p-methoxyphenylethylamine
Keywords keywords	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.

2hkr__assembly_1__model_1

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

Download this curve (.dat)

2hkr__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2hkr__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	30.56 Å
Rg (electron density)	30.01 Å
Total Rg	30.64 Å
Atom count	7383
Residues	950
Excluded volume	129900 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2hkr__assembly_1__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 (5)

Entity 1 Entity 1 polymer

Description description	Aromatic amine dehydrogenase, small subunit
Molecular weight formula_weight	13469.9 kDa
EC 编号 ec_number	1.4.99.4
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,H
Atom count atom_count	8897

HISLNPDLANEDEVNSCDYWRHCAVDGFLCSCCGGTTTTCPPGSTPSPISWIGTCHNPHDGKDYLISYHDCCGKTACGRCQCNTQTRERPGYEFFLHNDVNWCMANENSTFHCTTSVLVGLA

Entity 2 Entity 2 polymer

Description description	Aromatic amine dehydrogenase, large subunit
Molecular weight formula_weight	40113.2 kDa
EC 编号 ec_number	1.4.99.4
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B

PREVLTGGHSVSAPQENRIYVMDSVFMHLTESRVHVYDYTNGKFLGMVPTAFNGHVQVSNDGKKIYTMTTYHERITRGKRSDVVEVWDADKLTFEKEISLPPKRVQGLNYDGLFRQTTDGKFIVLQNASPATSIGIVDVAKGDYVEDVTAAAGCWSVIPQPNRPRSFMTICGDGGLLTINLGEDGKVASQSRSKQMFSVKDDPIFIAPALDKDKAHFVSYYGNVYSADFSGDEVKVDGPWSLLNDEDKAKNWVPGGYNLVGLHRASGRMYVFMHPDGKEGTHKFPAAEIWVMDTKTKQRVARIPGRDALSMTIDQQRNLMLTLDGGNVNVYDISQPEPKLLRTIEGAAEASLQVQFHPVGGT

Source Source

Source organism organism	Alcaligenes faecalis
NCBI taxonomy ID ncbi_taxonomy_id	511
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	2-(4-METHOXYPHENYL)ETHANAMINE
Molecular weight formula_weight	151.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	2-(4-METHOXYPHENYL)ACETAMIDE
Molecular weight formula_weight	165.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1383

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2hkrd_
Class class	g — Small proteins
Fold Fold fold	g.21 — Methylamine dehydrogenase, L chain
Superfamily Superfamily superfamily	g.21.1 — Methylamine dehydrogenase, L chain
Family Family family	g.21.1.0 — automated matches

Domain ID domain_id	d2hkrh_
Class class	g — Small proteins
Fold Fold fold	g.21 — Methylamine dehydrogenase, L chain
Superfamily Superfamily superfamily	g.21.1 — Methylamine dehydrogenase, L chain
Family Family family	g.21.1.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id	2hkrA01
Class class	2 — Mainly Beta
Architecture architecture	130 — 7 Propeller
Topology topology	10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily	10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

Domain ID domain_id	2hkrB01
Class class	2 — Mainly Beta
Architecture architecture	130 — 7 Propeller
Topology topology	10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily	10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

Domain ID domain_id	2hkrD00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	30 — Electron Transport Ethylamine Dehydrogenase
Homologous superfamily homologous superfamily	10 — Methylamine/Aralkylamine dehydrogenase light chain

Domain ID domain_id	2hkrH00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	30 — Electron Transport Ethylamine Dehydrogenase
Homologous superfamily homologous superfamily	10 — Methylamine/Aralkylamine dehydrogenase light chain

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Unit-cell length a length_a	70.848 Å
Unit-cell length b length_b	88.813 Å
Unit-cell length c length_c	80.044 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.39 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	1.400 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	—
R_work r_work	0.1490
R_free r_free	0.1710

Structures of the carbinolamine and schiff-base intermediates in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with p-methoxyphenylethylamine

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

Aromatic amine dehydrogenase, small subunit

State in the Current Structure

Other States of the Same Protein in the Database

Aromatic amine dehydrogenase, large subunit

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

2hkr__assembly_1__model_1

2hkr__assembly_1__model_1 | I(q)

2hkr__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

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) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Structures of the carbinolamine and schiff-base intermediates in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with p-methoxyphenylethylamine

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

Aromatic amine dehydrogenase, small subunit

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Aromatic amine dehydrogenase, large subunit

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

2hkr__assembly_1__model_1

2hkr__assembly_1__model_1 | I(q)

2hkr__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

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) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (1)