SAXSdb — 3axy

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

Protein HEADING DATE 3A

Oryza sativa Japonica Group

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	14-3-3-like protein GF14-C × 2 （Q6ZKC0） Rice FD homolog OsFD1 × 2 water × 6	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 6	14-3-3-like protein GF14-C × 2 （Q6ZKC0） Rice FD homolog OsFD1 × 2 water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HD3A_ORYSJ
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 6–170； UniProt 6–170 Author chain B； PDBConstruct 6–170； UniProt 6–170 Author chain G； PDBConstruct 6–170； UniProt 6–170 Author chain H； PDBConstruct 6–170； UniProt 6–170

14-3-3-like protein GF14-C

Oryza sativa Japonica Group

UniProt Q6ZKC0

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	Protein HEADING DATE 3A × 2 （Q93WI9） Rice FD homolog OsFD1 × 2 water × 6	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 6	Protein HEADING DATE 3A × 2 （Q93WI9） Rice FD homolog OsFD1 × 2 water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	14333_ORYSJ
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 6–240； UniProt 1–235 Author chain D； PDBConstruct 6–240； UniProt 1–235 Author chain I； PDBConstruct 6–240； UniProt 1–235 Author chain J； PDBConstruct 6–240； UniProt 1–235

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	3axy
Deposition date deposition_date	2011-04-19
Structure title title	Structure of Florigen Activation Complex Consisting of Rice Florigen Hd3a, 14-3-3 Protein GF14 and Rice FD Homolog OsFD1
Keywords keywords	;Phosphatidylethanolamine-binding Protein, 14-3-3 Protein, bZip protein, Floral Induction, Transcriptional Activator, Signaling Protein, DNA Binding, Phosphorylation, Nucleus, SIGNALING PROTEIN-PROTEIN BINDING complex ;; SIGNALING PROTEIN/PROTEIN BINDING
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.

3axy__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3axy__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3axy__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	36.11 Å
Rg (electron density)	35.21 Å
Total Rg	35.69 Å
Atom count	6480
Residues	812
Excluded volume	115210 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3axy__assembly_1__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3axy__assembly_2__model_1`	hexameric （6）	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	Protein HEADING DATE 3A
Molecular weight formula_weight	18982.4 kDa
Mutation mutation	C43L,C109S,C166S
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,G,H
Atom count atom_count	13751

GPGHMRDRDPLVVGRVVGDVLDAFVRSTNLKVTYGSKTVSNGLELKPSMVTHQPRVEVGGNDMRTFYTLVMVDPDAPSPSDPNLREYLHWLVTDIPGTTAASFGQEVMSYESPRPTMGIHRLVFVLFQQLGRQTVYAPGWRQNFNTKDFAELYNLGSPVAAVYFNSQREA

Source Source

Source organism organism	Oryza sativa Japonica Group
Common name common_name	Japanese rice
NCBI taxonomy ID ncbi_taxonomy_id	39947
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	14-3-3-like protein GF14-C
Molecular weight formula_weight	27151.8 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D,I,J

GPLGSMSREENVYMAKLAEQAERYEEMVEYMEKVAKTVDVEELTVEERNLLSVAYKNVIGARRASWRIVSSIEQKEEGRGNEEHVTLIKEYRGKIEAELSKICDGILKLLDSHLVPSSTAAESKVFYLKMKGDYHRYLAEFKTGAERKEAAESTMVAYKAAQDIALADLAPTHPIRLGLALNFSVFYYEILNSPDKACNLAKQAFDEAISELDTLGEESYKDSTLIMQLLRDNLTLWTSD

Source Source

Source organism organism	Oryza sativa Japonica Group
Common name common_name	Japanese rice
NCBI taxonomy ID ncbi_taxonomy_id	39947
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Rice FD homolog OsFD1
Molecular weight formula_weight	1111.2 kDa
Source method src_method	syn
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,K,L

LQRVLSAPF

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	777

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3axyc_
Class class	a — All alpha proteins
Fold Fold fold	a.118 — alpha-alpha superhelix
Superfamily Superfamily superfamily	a.118.7 — 14-3-3 protein
Family Family family	a.118.7.1 — 14-3-3 protein

Domain ID domain_id	d3axyd_
Class class	a — All alpha proteins
Fold Fold fold	a.118 — alpha-alpha superhelix
Superfamily Superfamily superfamily	a.118.7 — 14-3-3 protein
Family Family family	a.118.7.1 — 14-3-3 protein

Domain ID domain_id	d3axyi_
Class class	a — All alpha proteins
Fold Fold fold	a.118 — alpha-alpha superhelix
Superfamily Superfamily superfamily	a.118.7 — 14-3-3 protein
Family Family family	a.118.7.1 — 14-3-3 protein

Domain ID domain_id	d3axyj_
Class class	a — All alpha proteins
Fold Fold fold	a.118 — alpha-alpha superhelix
Superfamily Superfamily superfamily	a.118.7 — 14-3-3 protein
Family Family family	a.118.7.1 — 14-3-3 protein

CATH v4.4 (8 domains)

Domain ID domain_id	3axyA00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	280 — Phosphatidylethanolamine-binding Protein
Homologous superfamily homologous superfamily	10 — PEBP-like

Domain ID domain_id	3axyB00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	280 — Phosphatidylethanolamine-binding Protein
Homologous superfamily homologous superfamily	10 — PEBP-like

Domain ID domain_id	3axyC00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	20 — 14-3-3 domain

Domain ID domain_id	3axyD00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	20 — 14-3-3 domain

Domain ID domain_id	3axyG00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	280 — Phosphatidylethanolamine-binding Protein
Homologous superfamily homologous superfamily	10 — PEBP-like

Domain ID domain_id	3axyH00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	280 — Phosphatidylethanolamine-binding Protein
Homologous superfamily homologous superfamily	10 — PEBP-like

Domain ID domain_id	3axyI00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	20 — 14-3-3 domain

Domain ID domain_id	3axyJ00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	20 — 14-3-3 domain

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Unit-cell length a length_a	76.735 Å
Unit-cell length b length_b	96.647 Å
Unit-cell length c length_c	99.510 Å
Unit-cell angle α angle_alpha	68.23 °
Unit-cell angle β angle_beta	87.90 °
Unit-cell angle γ angle_gamma	77.94 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.2308
R_work r_work	0.2273
R_free r_free	0.2763

Structure of Florigen Activation Complex Consisting of Rice Florigen Hd3a, 14-3-3 Protein GF14 and Rice FD Homolog OsFD1

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

Protein HEADING DATE 3A

State in the Current Structure

Other States of the Same Protein in the Database

14-3-3-like protein GF14-C

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

3axy__assembly_2__model_1

3axy__assembly_2__model_1 | I(q)

3axy__assembly_2__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 polymer

Polymer Polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (1)

Structure of Florigen Activation Complex Consisting of Rice Florigen Hd3a, 14-3-3 Protein GF14 and Rice FD Homolog OsFD1

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

Protein HEADING DATE 3A

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

14-3-3-like protein GF14-C

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

3axy__assembly_2__model_1

3axy__assembly_2__model_1 | I(q)

3axy__assembly_2__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 polymer

Polymer Polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (1)