SAXSdb — 5vy5

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

Fructose-bisphosphate aldolase A

Oryctolagus cuniculus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ALDOA_RABIT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–363； UniProt 2–364 Author chain B； PDBConstruct 1–363； UniProt 2–364 Author chain C； PDBConstruct 1–363； UniProt 2–364 Author chain D； PDBConstruct 1–363； UniProt 2–364

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	5vy5
Deposition date deposition_date	2017-05-24
Structure title title	Rabbit muscle aldolase using 200keV
Keywords keywords	glycolytic enzyme, LYASE; LYASE
Experimental Method method	ELECTRON MICROSCOPY

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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.

5vy5__assembly_1__model_3

Assembly 1 · Model 3 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5vy5__assembly_1__model_3 | I(q)

100 plotted points; both axes use logarithmic scales.

5vy5__assembly_1__model_3 | P(r) · Pending

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

Rg（Guinier）	35.51 Å
Rg (electron density)	34.72 Å
Total Rg	35.15 Å
Atom count	10472
Residues	1372
Excluded volume	186590 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5vy5__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	2	`5vy5__assembly_1__model_2`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	3	`5vy5__assembly_1__model_3`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	4	`5vy5__assembly_1__model_4`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	5	`5vy5__assembly_1__model_5`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	6	`5vy5__assembly_1__model_6`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	7	`5vy5__assembly_1__model_7`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	8	`5vy5__assembly_1__model_8`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	9	`5vy5__assembly_1__model_9`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	10	`5vy5__assembly_1__model_10`	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 (1)

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d5vy5a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.10 — Aldolase
Family Family family	c.1.10.1 — Class I aldolase

Domain ID domain_id	d5vy5b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.10 — Aldolase
Family Family family	c.1.10.1 — Class I aldolase

Domain ID domain_id	d5vy5c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.10 — Aldolase
Family Family family	c.1.10.1 — Class I aldolase

Domain ID domain_id	d5vy5d_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.10 — Aldolase
Family Family family	c.1.10.1 — Class I aldolase

CATH v4.4 (4 domains)

Domain ID domain_id	5vy5A00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	5vy5B00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	5vy5C00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	5vy5D00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

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

Resolution resolution	2.60 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	83910

Description description	Fructose-bisphosphate aldolase A
Molecular weight formula_weight	39263.7 kDa
EC 编号 ec_number	4.1.2.13
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,A,C,D
Atom count atom_count	104720

Rabbit muscle aldolase using 200keV

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

Fructose-bisphosphate aldolase A

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

5vy5__assembly_1__model_3

5vy5__assembly_1__model_3 | I(q)

5vy5__assembly_1__model_3 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Source organism organism	Oryctolagus cuniculus
Common name common_name	Rabbit
NCBI taxonomy ID ncbi_taxonomy_id	9986
Host organism host_organism	Escherichia coli

Rabbit muscle aldolase using 200keV

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

Fructose-bisphosphate aldolase A

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

5vy5__assembly_1__model_3

5vy5__assembly_1__model_3 | I(q)

5vy5__assembly_1__model_3 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)