SAXSdb — 1eo2

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

PROTOCATECHUATE 3,4-DIOXYGENASE ALPHA CHAIN

Acinetobacter sp.

UniProt P20371

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 24	PROTOCATECHUATE 3,4-DIOXYGENASE BETA CHAIN × 12 （P20372） FE (III) ION × 12 water × 24	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PCXA_ACIAD
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–209； UniProt 1–209

PROTOCATECHUATE 3,4-DIOXYGENASE BETA CHAIN

Acinetobacter sp.

UniProt P20372

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 24	PROTOCATECHUATE 3,4-DIOXYGENASE ALPHA CHAIN × 12 （P20371） FE (III) ION × 12 water × 24	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PCXB_ACIAD
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–241； UniProt 1–241

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	1eo2
Deposition date deposition_date	2000-03-21
Structure title title	CRYSTAL STRUCTURE OF ACINETOBACTER SP. ADP1 PROTOCATECHUATE 3,4-DIOXYGENASE
Keywords keywords	beta-sandwich, mixed alpha/beta structure, dioxygenase, biodegradation, 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.

1eo2__assembly_1__model_1

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

Download this curve (.dat)

1eo2__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1eo2__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	54.27 Å
Rg (electron density)	53.21 Å
Total Rg	53.47 Å
Atom count	42348
Residues	5280
Excluded volume	744880 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1eo2__assembly_1__model_1`	24-meric （24）	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	PROTOCATECHUATE 3,4-DIOXYGENASE ALPHA CHAIN
Molecular weight formula_weight	23508.1 kDa
EC 编号 ec_number	1.13.11.3
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	3712

MNGWNFQELKETPSQTGGPYVHIGLLPKQANIEVFEHNLDNNLVQDNTQGQRIRLEGQVFDGLGLPLRDVLIEIWQADTNGVYPSQADTQGKQVDPNFLGWGRTGADFGTGFWSFNTIKPGAVPGRKGSTQAPHISLIIFARGINIGLHTRVYFDDEAEANAKDPVLNSIEWATRRQTLVAKREERDGEVVYRFDIRIQGENETVFFDI

Source Source

Source organism organism	Acinetobacter sp.
NCBI taxonomy ID ncbi_taxonomy_id	62977
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	PROTOCATECHUATE 3,4-DIOXYGENASE BETA CHAIN
Molecular weight formula_weight	27583.0 kDa
EC 编号 ec_number	1.13.11.3
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MSQIIWGAYAQRNTEDHPPAYAPGYKTSVLRSPKNALISIAETLSEVTAPHFSADKFGPKDNDLILNYAKDGLPIGERVIVHGYVRDQFGRPVKNALVEVWQANASGRYRHPNDQYIGAMDPNFGGCGRMLTDDNGYYVFRTIKPGPYPWRNRINEWRPAHIHFSLIADGWAQRLISQFYFEGDTLIDSCPILKTIPSEQQRRALIALEDKSNFIEADSRCYRFDITLRGRRATYFENDLT

Source Source

Source organism organism	Acinetobacter sp.
NCBI taxonomy ID ncbi_taxonomy_id	62977
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	FE (III) ION
Molecular weight formula_weight	55.8 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	183

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1eo2a_
Class class	b — All beta proteins
Fold Fold fold	b.3 — Prealbumin-like
Superfamily Superfamily superfamily	b.3.6 — Aromatic compound dioxygenase
Family Family family	b.3.6.1 — Aromatic compound dioxygenase

Domain ID domain_id	d1eo2b_
Class class	b — All beta proteins
Fold Fold fold	b.3 — Prealbumin-like
Superfamily Superfamily superfamily	b.3.6 — Aromatic compound dioxygenase
Family Family family	b.3.6.1 — Aromatic compound dioxygenase

CATH v4.4 (2 domains)

Domain ID domain_id	1eo2A00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	130 — Protocatechuate 3,4-Dioxygenase, subunit A
Homologous superfamily homologous superfamily	10 — Aromatic compound dioxygenase

Domain ID domain_id	1eo2B00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	130 — Protocatechuate 3,4-Dioxygenase, subunit A
Homologous superfamily homologous superfamily	10 — Aromatic compound dioxygenase

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Unit-cell length a length_a	145.500 Å
Unit-cell length b length_b	145.500 Å
Unit-cell length c length_c	145.500 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	24

Space group space_group	I 2 3
Space-group number int_tables_number	197
Crystal system crystal_system	—

Resolution resolution	2.250 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1760
R_work r_work	0.1760
R_free r_free	0.2180

CRYSTAL STRUCTURE OF ACINETOBACTER SP. ADP1 PROTOCATECHUATE 3,4-DIOXYGENASE

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

PROTOCATECHUATE 3,4-DIOXYGENASE ALPHA CHAIN

State in the Current Structure

Other States of the Same Protein in the Database

PROTOCATECHUATE 3,4-DIOXYGENASE BETA CHAIN

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

1eo2__assembly_1__model_1

1eo2__assembly_1__model_1 | I(q)

1eo2__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 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (5)

CRYSTAL STRUCTURE OF ACINETOBACTER SP. ADP1 PROTOCATECHUATE 3,4-DIOXYGENASE

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

PROTOCATECHUATE 3,4-DIOXYGENASE ALPHA CHAIN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

PROTOCATECHUATE 3,4-DIOXYGENASE BETA CHAIN

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

1eo2__assembly_1__model_1

1eo2__assembly_1__model_1 | I(q)

1eo2__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 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (5)