SAXSdb — 2c63

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

14-3-3 PROTEIN ETA

HOMO SAPIENS

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–245 Chain B； UniProt 1–245	Not recorded	CONSENSUS PEPTIDE FOR 14-3-3 PROTEINS × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；0.2M MGCL2, 0.1M HEPES PH 7.5, 25% PEG 3350	Resolution 2.15 Å R-free 0.248
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain C； UniProt 1–245 Chain D； UniProt 1–245	Not recorded	CONSENSUS PEPTIDE FOR 14-3-3 PROTEINS × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；0.2M MGCL2, 0.1M HEPES PH 7.5, 25% PEG 3350	Resolution 2.15 Å R-free 0.248

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 2C63	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2C74 14-3-3 Protein Eta (Human) Complexed to Peptide Deposited 2005-11-17	Different ligand/ion 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	CIT CITRIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；0.1M CITRATE PH 5.6, 20% ISOPROPANOL, 20% PEG4000	Resolution 2.70 Å R-free 0.291
7NMZ Structure of 14-3-3 eta in complex with Nedd4-2(335-455) containing two 14-3-3 binding motifs Ser342 and Ser448 Deposited 2021-02-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain AA 1–234（234 aa） Chain BA 1–234（234 aa）	Mutation：S235Stop Mutation：S235Stop	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293.15 K；12.5% w/v PEG 1000, 12.5% w/v PEG 3350, 12.5% v/v MPD, 0.03M of each NPS (sodium nitrate, sodium phosphate dibasic, ammonium sulfate), 0.1Mbicine/Trizma base pH 8.5, 30% sacharose	Resolution 2.30 Å R-free 0.235
9R2I Cryo-EM structure of the complex CDK16:CCNY:14-3-3 Deposited 2025-04-30	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–246（246 aa） Chain B 1–246（246 aa）	Not recorded	MG MAGNESIUM ION × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8；20 mM HEPES buffer (pH 8.0), 150 mM NaCl, 4 mM MgCl2, 0.5 mM TCEP and 7.8 mM CHAPSO and supplemented with 2 mM ATP-gamma-S cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9R2N Cryo-EM structure of the complex CCNY:14-3-3 Deposited 2025-04-30	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–246（246 aa） Chain B 1–246（246 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8；20 mM HEPES buffer (pH 8.0), 150 mM NaCl, 4 mM MgCl2, 0.5 mM TCEP and 7.8 mM CHAPSO cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.83 Å

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

View Construct and Data Evidence

UniProt name	1433F_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–247； UniProt 1–245 Author chain B； PDBConstruct 3–247； UniProt 1–245 Author chain C； PDBConstruct 3–247； UniProt 1–245 Author chain D； PDBConstruct 3–247； 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	2c63
Deposition date deposition_date	2005-11-07
Structure title title	14-3-3 Protein Eta (Human) Complexed to Peptide
Keywords keywords	;SIGNALING PROTEIN-PEPTIDE COMPLEX, 14-3-3, PHOSPHOSERINE, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, PHOSPHORYLATION, YWHAH ;; SIGNALING PROTEIN/PEPTIDE
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	33.86 Å
Radius of gyration Rg (electron density) rg_electron	33.24 Å
Forward intensity I(0) i0	179627000.00
Molecular weight molecular_weight	106560.0 kDa
Excluded volume excluded_volume	133040 Å³
Envelope volume envelope_volume	178800 Å³
Hydration-shell volume shell_volume	45211 Å³
Envelope diameter envelope_diameter	113.7 Å
Shell Rg shell_rg	40.11 Å
Envelope Rg envelope_rg	32.53 Å
Shape Rg shape_rg	33.27 Å
Total Rg total_rg	33.68 Å
Total atoms total_atoms	7489
Residues n_residues	944
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	106.6 Å
Rg (real space) rg_real	33.71 Å
Rg uncertainty (real space) rg_real_error	0.90 Å
I(0) (real space) i0_real	1.7960e+08
I(0) uncertainty (real space) i0_real_error	2.7920e+06
Rg (reciprocal space) rg_reciprocal	33.80 Å
I(0) (reciprocal space) i0_reciprocal	179600000.0000
Solution quality estimate total_estimate	0.8972
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	43.1 Å
Skewness Skewness skewness	0.129
Kurtosis Kurtosis kurtosis	-0.445
Angular range angular_range	— – 0.2350 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	12560000.0000
Real-space data points n_real_points	48
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.915; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.918

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	14-3-3 PROTEIN ETA
Molecular weight formula_weight	28338.8 kDa
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	7886

SMGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSSWRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLSLLDKFLIKNCNDFQYESKVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEQMQPTHPIRLGLALNFSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDEEAGEGN

来源 Source

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	CONSENSUS PEPTIDE FOR 14-3-3 PROTEINS
Molecular weight formula_weight	736.8 kDa
Source method src_method	syn
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	P,Q,R,S

RAISLP

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	397

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7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	2c63A00
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	2c63B00
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	2c63C00
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	2c63D00
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	58.251 Å
Unit-cell length b length_b	79.398 Å
Unit-cell length c length_c	125.109 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	95.15 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.150 Å
Low-resolution limit resolution_low	125.000 Å
R factor r_factor	0.1850
R_work r_work	0.1840
R_free r_free	0.2480

fit	/app/data/saxs_computation/c6/2c63/2c63.fit
pddf	/app/data/pr_computation/c6/2c63/2c63.pr.out
profile	/app/data/saxs_computation/c6/2c63/2c63.dat

14-3-3 Protein Eta (Human) Complexed to Peptide

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

14-3-3 PROTEIN ETA

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)