SAXSdb — 2hi7

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

Thiol:disulfide interchange protein dsbA

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Disulfide bond formation protein B × 1 （P0A6M2） ZINC ION × 1 UBIQUINONE-1 × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 4	Disulfide bond formation protein B × 2 （P0A6M2） ZINC ION × 2 UBIQUINONE-1 × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	DSBA_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–189； UniProt 20–208

Disulfide bond formation protein B

Escherichia coli

UniProt P0A6M2

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Thiol:disulfide interchange protein dsbA × 1 （P0AEG4） ZINC ION × 1 UBIQUINONE-1 × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 4	Thiol:disulfide interchange protein dsbA × 2 （P0AEG4） ZINC ION × 2 UBIQUINONE-1 × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	DSBB_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–176； UniProt 1–176

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	2hi7
Deposition date deposition_date	2006-06-29
Structure title title	Crystal structure of DsbA-DsbB-ubiquinone complex
Keywords keywords	disulfide bond, redox, DsbB, membrane protein, ubiquinone, oxidative protein folding, 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.

2hi7__assembly_1__model_1

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

Download this curve (.dat)

2hi7__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2hi7__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	23.27 Å
Rg (electron density)	23.05 Å
Total Rg	23.92 Å
Atom count	2575
Residues	322
Excluded volume	46869 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2hi7__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2hi7__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 (4)

Entity 1 Entity 1 polymer

Description description	Thiol:disulfide interchange protein dsbA
Molecular weight formula_weight	21123.0 kDa
EC 编号 ec_number	1.8.4.-
Mutation mutation	C33A
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2575

AQYEDGKQYTTLEKPVAGAPQVLEFFSFFCPHAYQFEEVLHISDNVKKKLPEGVKMTKYHVNFMGGDLGKDLTQAWAVAMALGVEDKVTVPLFEGVQKTQTIRSASDIRDVFINAGIKGEEYDAAWNSFVVKSLVAQQEKAAADVQLRGVPAMFVNGKYQLNPQGMDTSNMDVFVQQYADTVKYLSEKK

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Disulfide bond formation protein B
Molecular weight formula_weight	20107.0 kDa
EC 编号 ec_number	1.8.5.-
Mutation mutation	C8A,C49V,C130S
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MLRFLNQASQGRGAWLLMAFTALALELTALWFQHVMLLKPCVLCIYERVALFGVLGAALIGAIAPKTPLRYVAMVIWLYSAFRGVQLTYEHTMLQLYPSPFATCDFMVRFPEWLPLDKWVPQVFVASGDSAERQWDFLGLEMPQWLLGIFIAYLIVAVLVVISQPFKAKKRDLFGR

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	UBIQUINONE-1
Molecular weight formula_weight	250.3 kDa
Source method src_method	syn
Copy count entity_count	1

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2hi7a1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.47 — Thioredoxin fold
Superfamily Superfamily superfamily	c.47.1 — Thioredoxin-like
Family Family family	c.47.1.13 — DsbA-like

Domain ID domain_id	d2hi7b1
Class class	a — All alpha proteins
Fold Fold fold	a.29 — Bromodomain-like
Superfamily Superfamily superfamily	a.29.15 — DsbB-like
Family Family family	a.29.15.1 — DsbB-like

CATH v4.4 (2 domains)

Domain ID domain_id	2hi7A00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	2hi7B00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1550 — Bromodomain-like
Homologous superfamily homologous superfamily	10 — DsbB-like

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Unit-cell length a length_a	165.500 Å
Unit-cell length b length_b	165.500 Å
Unit-cell length c length_c	65.920 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 42 21 2
Space-group number int_tables_number	94
Crystal system crystal_system	—

Resolution resolution	3.700 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.3422
R_work r_work	0.3412
R_free r_free	0.3615

Crystal structure of DsbA-DsbB-ubiquinone complex

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

Thiol:disulfide interchange protein dsbA

State in the Current Structure

Other States of the Same Protein in the Database

Disulfide bond formation protein B

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

2hi7__assembly_1__model_1

2hi7__assembly_1__model_1 | I(q)

2hi7__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 (4)

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

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Crystal structure of DsbA-DsbB-ubiquinone complex

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

Thiol:disulfide interchange protein dsbA

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Disulfide bond formation protein B

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

2hi7__assembly_1__model_1

2hi7__assembly_1__model_1 | I(q)

2hi7__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 (4)

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

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)