SAXSdb — 6zbt

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

14-3-3 protein gamma

Homo sapiens

UniProt P61981

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	E3 ubiquitin-protein ligase NEDD4-like × 2 （Q96PU5） 1,1,1,3,3,3-hexafluoropropan-2-ol × 3 water × 4	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 4	E3 ubiquitin-protein ligase NEDD4-like × 2 （Q96PU5） 1,1,1,3,3,3-hexafluoropropan-2-ol × 1 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	1433G_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–234； UniProt 1–234 Author chain B； PDBConstruct 1–234； UniProt 1–234 Author chain C； PDBConstruct 1–234； UniProt 1–234 Author chain D； PDBConstruct 1–234； UniProt 1–234

E3 ubiquitin-protein ligase NEDD4-like

OrganismNot specified

UniProt Q96PU5

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	14-3-3 protein gamma × 2 （P61981） 1,1,1,3,3,3-hexafluoropropan-2-ol × 3 water × 4	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 4	14-3-3 protein gamma × 2 （P61981） 1,1,1,3,3,3-hexafluoropropan-2-ol × 1 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	NED4L_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–10； UniProt 338–347 Author chain F； PDBConstruct 1–10； UniProt 338–347 Author chain G； PDBConstruct 1–10； UniProt 338–347 Author chain H； PDBConstruct 1–10； UniProt 338–347

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	6zbt
Deposition date deposition_date	2020-06-09
Structure title title	Structure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser342
Keywords keywords	E3 ubiquitin protein ligase, complex, phosphorylation, 14-3-3 protein, signaling protein; SIGNALING PROTEIN
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.

6zbt__assembly_2__model_1

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

Download this curve (.dat)

6zbt__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6zbt__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	27.85 Å
Rg (electron density)	27.04 Å
Total Rg	27.70 Å
Atom count	3674
Residues	467
Excluded volume	64946 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6zbt__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`6zbt__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	14-3-3 protein gamma
Molecular weight formula_weight	27004.4 kDa
Mutation mutation	S235Stop
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	8014

MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWT

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	E3 ubiquitin-protein ligase NEDD4-like
Molecular weight formula_weight	1131.2 kDa
EC 编号 ec_number	2.3.2.26
Source method src_method	syn
Copy count entity_count	4

Polymer Polymer

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

LRSCSVTDAV

Entity 3 Entity 3 non-polymer

Description description	1,1,1,3,3,3-hexafluoropropan-2-ol
Molecular weight formula_weight	168.0 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	642

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	6zbtA01
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	6zbtB01
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	6zbtC01
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	6zbtD01
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	205.857 Å
Unit-cell length b length_b	205.857 Å
Unit-cell length c length_c	74.354 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	36

Space group space_group	H 3
Space-group number int_tables_number	146
Crystal system crystal_system	trigonal

Resolution resolution	1.799 Å
Low-resolution limit resolution_low	27.510 Å
R factor r_factor	0.2107
R_work r_work	0.2101
R_free r_free	0.2405

Structure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser342

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

14-3-3 protein gamma

State in the Current Structure

Other States of the Same Protein in the Database

E3 ubiquitin-protein ligase NEDD4-like

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

6zbt__assembly_2__model_1

6zbt__assembly_2__model_1 | I(q)

6zbt__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

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)

Structure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser342

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

14-3-3 protein gamma

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

E3 ubiquitin-protein ligase NEDD4-like

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

6zbt__assembly_2__model_1

6zbt__assembly_2__model_1 | I(q)

6zbt__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

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)