SAXSdb — 1a4o

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

14-3-3 PROTEIN ZETA

Bos taurus

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–245 Chain B； UniProt 1–245	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；pH 8.5	Resolution 2.80 Å R-free 0.345
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–245 Chain D； UniProt 1–245	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；pH 8.5	Resolution 2.80 Å R-free 0.345

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1A4O	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A37 14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE Deposited 1998-01-28	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–245（245 aa） Chain B 1–245（245 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 3.60 Å R-free 0.360
1A38 14-3-3 PROTEIN ZETA BOUND TO R18 PEPTIDE Deposited 1998-01-28	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–245（245 aa） Chain B 1–245（245 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 3.35 Å R-free 0.390
2V7D 14-3-3 protein zeta in complex with Thr758 phosphorylated integrin beta2 peptide Deposited 2007-07-30	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–245（245 aa） Chain B 1–245（245 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；18-19% PEG3350, 10MM CACL2, 1MM NICL2, 100MM TRIS PH8.5	Resolution 2.50 Å R-free 0.273
2V7D 14-3-3 protein zeta in complex with Thr758 phosphorylated integrin beta2 peptide Deposited 2007-07-30	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–245（245 aa） Chain D 1–245（245 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；18-19% PEG3350, 10MM CACL2, 1MM NICL2, 100MM TRIS PH8.5	Resolution 2.50 Å R-free 0.273

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	1433Z_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–245； UniProt 1–245 Author chain B； PDBConstruct 1–245； UniProt 1–245 Author chain C； PDBConstruct 1–245； UniProt 1–245 Author chain D； PDBConstruct 1–245； UniProt 1–245

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	1a4o
Deposition date deposition_date	1998-02-01
Structure title title	14-3-3 PROTEIN ZETA ISOFORM
Keywords keywords	SIGNAL TRANSDUCTION; SIGNAL TRANSDUCTION
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	30.92 Å
Radius of gyration Rg (electron density) rg_electron	30.49 Å
Forward intensity I(0) i0	130454000.00
Molecular weight molecular_weight	90700.0 kDa
Excluded volume excluded_volume	113800 Å³
Envelope volume envelope_volume	153350 Å³
Hydration-shell volume shell_volume	42215 Å³
Envelope diameter envelope_diameter	106.9 Å
Shell Rg shell_rg	37.48 Å
Envelope Rg envelope_rg	30.24 Å
Shape Rg shape_rg	30.50 Å
Total Rg total_rg	31.11 Å
Total atoms total_atoms	6360
Residues n_residues	788
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	102.1 Å
Rg (real space) rg_real	30.78 Å
Rg uncertainty (real space) rg_real_error	0.69 Å
I(0) (real space) i0_real	1.3050e+08
I(0) uncertainty (real space) i0_real_error	2.0850e+06
Rg (reciprocal space) rg_reciprocal	30.84 Å
I(0) (reciprocal space) i0_reciprocal	130500000.0000
Solution quality estimate total_estimate	0.8872
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	38.0 Å
Skewness Skewness skewness	0.211
Kurtosis Kurtosis kurtosis	-0.334
Angular range angular_range	— – 0.2550 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	11840000.0000
Real-space data points n_real_points	52
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.848; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.986

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1a4oa_
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	d1a4ob_
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	d1a4oc_
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	d1a4od_
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 (4 domains)

Domain ID domain_id	1a4oA00
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	1a4oB00
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	1a4oC00
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	1a4oD00
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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8. Citations (1)

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Unit-cell length a length_a	94.900 Å
Unit-cell length b length_b	94.900 Å
Unit-cell length c length_c	236.700 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	24

Space group space_group	P 65
Space-group number int_tables_number	170
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.3100
R_work r_work	0.3100
R_free r_free	0.3450

Description description	14-3-3 PROTEIN ZETA
Molecular weight formula_weight	27777.1 kDa
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	6360

14-3-3 PROTEIN ZETA ISOFORM

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

14-3-3 PROTEIN ZETA

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Bos taurus
通用名 common_name	cattle
NCBI Class编号 ncbi_taxonomy_id	9913
宿主生物 host_organism	Escherichia coli

fit	/app/data/saxs_computation/a4/1a4o/1a4o.fit
pddf	/app/data/pr_computation/a4/1a4o/1a4o.pr.out
profile	/app/data/saxs_computation/a4/1a4o/1a4o.dat