SAXSdb — 2o70

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

OHCU decarboxylase

Danio rerio

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A1L259_BRARE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–174； UniProt 1–174 Author chain B； PDBConstruct 1–174； UniProt 1–174 Author chain C； PDBConstruct 1–174； UniProt 1–174 Author chain D； PDBConstruct 1–174； UniProt 1–174 Author chain E； PDBConstruct 1–174； UniProt 1–174 Author chain F； PDBConstruct 1–174； UniProt 1–174

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	2o70
Deposition date deposition_date	2006-12-09
Structure title title	Structure of OHCU decarboxylase from zebrafish
Keywords keywords	Uric acid, decarboxylation, 5-hydroxyisourate, allantoin, LYASE; LYASE
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.

2o70__assembly_1__model_1

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

Download this curve (.dat)

2o70__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2o70__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	21.95 Å
Rg (electron density)	20.85 Å
Total Rg	21.75 Å
Atom count	2619
Residues	329
Excluded volume	46578 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2o70__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2o70__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2o70__assembly_3__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 (2)

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d2o70a1
Class class	a — All alpha proteins
Fold Fold fold	a.288 — UraD-like
Superfamily Superfamily superfamily	a.288.1 — UraD-Like
Family Family family	a.288.1.1 — UraD-like

Domain ID domain_id	d2o70b_
Class class	a — All alpha proteins
Fold Fold fold	a.288 — UraD-like
Superfamily Superfamily superfamily	a.288.1 — UraD-Like
Family Family family	a.288.1.1 — UraD-like

Domain ID domain_id	d2o70c_
Class class	a — All alpha proteins
Fold Fold fold	a.288 — UraD-like
Superfamily Superfamily superfamily	a.288.1 — UraD-Like
Family Family family	a.288.1.1 — UraD-like

Domain ID domain_id	d2o70d_
Class class	a — All alpha proteins
Fold Fold fold	a.288 — UraD-like
Superfamily Superfamily superfamily	a.288.1 — UraD-Like
Family Family family	a.288.1.1 — UraD-like

Domain ID domain_id	d2o70e_
Class class	a — All alpha proteins
Fold Fold fold	a.288 — UraD-like
Superfamily Superfamily superfamily	a.288.1 — UraD-Like
Family Family family	a.288.1.1 — UraD-like

Domain ID domain_id	d2o70f_
Class class	a — All alpha proteins
Fold Fold fold	a.288 — UraD-like
Superfamily Superfamily superfamily	a.288.1 — UraD-Like
Family Family family	a.288.1.1 — UraD-like

CATH v4.4 (6 domains)

Domain ID domain_id	2o70A00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3330 — UraD-like
Homologous superfamily homologous superfamily	10 — Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase

Domain ID domain_id	2o70B00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3330 — UraD-like
Homologous superfamily homologous superfamily	10 — Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase

Domain ID domain_id	2o70C00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3330 — UraD-like
Homologous superfamily homologous superfamily	10 — Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase

Domain ID domain_id	2o70D00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3330 — UraD-like
Homologous superfamily homologous superfamily	10 — Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase

Domain ID domain_id	2o70E00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3330 — UraD-like
Homologous superfamily homologous superfamily	10 — Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase

Domain ID domain_id	2o70F00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3330 — UraD-like
Homologous superfamily homologous superfamily	10 — Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase

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Unit-cell length a length_a	101.815 Å
Unit-cell length b length_b	101.815 Å
Unit-cell length c length_c	103.915 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	18

Space group space_group	P 32
Space-group number int_tables_number	145
Crystal system crystal_system	—

Resolution resolution	1.800 Å
Low-resolution limit resolution_low	67.000 Å
R factor r_factor	0.1978
R_work r_work	0.1955
R_free r_free	0.2402

Description description	OHCU decarboxylase
Molecular weight formula_weight	19768.6 kDa
Source method src_method	man
Copy count entity_count	6

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	9119

Structure of OHCU decarboxylase from zebrafish

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

OHCU decarboxylase

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

2o70__assembly_1__model_1

2o70__assembly_1__model_1 | I(q)

2o70__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (1)

Source organism organism	Danio rerio
Common name common_name	zebrafish
NCBI taxonomy ID ncbi_taxonomy_id	7955
Host organism host_organism	Escherichia coli BL21

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1224

Structure of OHCU decarboxylase from zebrafish

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

OHCU decarboxylase

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

2o70__assembly_1__model_1

2o70__assembly_1__model_1 | I(q)

2o70__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (1)