SAXSdb — 1a37

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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 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	PS-RAF259 PEPTIDE LSQRQRST(SEP)TPNVHM × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；pH 8.5	Resolution 3.60 Å R-free 0.360

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 1A37	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A38 14-3-3 PROTEIN ZETA BOUND TO R18 PEPTIDE Deposited 1998-01-28	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
1A4O 14-3-3 PROTEIN ZETA ISOFORM Deposited 1998-02-01	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	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 2.80 Å R-free 0.345
1A4O 14-3-3 PROTEIN ZETA ISOFORM Deposited 1998-02-01	Different oligomeric state Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	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；pH 8.5	Resolution 2.80 Å R-free 0.345
2V7D 14-3-3 protein zeta in complex with Thr758 phosphorylated integrin beta2 peptide Deposited 2007-07-30	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 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 5 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

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	1a37
Deposition date deposition_date	1998-01-28
Structure title title	14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE
Keywords keywords	SIGNAL TRANSDUCTION, COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE), COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE) complex; COMPLEX (SIGNAL TRANSDUCTION/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	26.05 Å
Radius of gyration Rg (electron density) rg_electron	25.43 Å
Forward intensity I(0) i0	36249200.00
Molecular weight molecular_weight	45557.0 kDa
Excluded volume excluded_volume	56675 Å³
Envelope volume envelope_volume	73528 Å³
Hydration-shell volume shell_volume	24233 Å³
Envelope diameter envelope_diameter	83.4 Å
Shell Rg shell_rg	32.42 Å
Envelope Rg envelope_rg	25.14 Å
Shape Rg shape_rg	25.44 Å
Total Rg total_rg	26.20 Å
Total atoms total_atoms	3194
Residues n_residues	402
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	80.5 Å
Rg (real space) rg_real	26.01 Å
Rg uncertainty (real space) rg_real_error	0.48 Å
I(0) (real space) i0_real	3.6250e+07
I(0) uncertainty (real space) i0_real_error	4.9330e+05
Rg (reciprocal space) rg_reciprocal	26.03 Å
I(0) (reciprocal space) i0_reciprocal	36250000.0000
Solution quality estimate total_estimate	0.9120
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	31.7 Å
Skewness Skewness skewness	0.222
Kurtosis Kurtosis kurtosis	-0.617
Angular range angular_range	— – 0.3050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7838000.0000
Real-space data points n_real_points	62
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.971; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.952

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	14-3-3 PROTEIN ZETA
Molecular weight formula_weight	27777.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3194

MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN

来源 Source

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

Entity 2 Entity 2 polymer

Description description	PS-RAF259 PEPTIDE LSQRQRST(SEP)TPNVHM
Molecular weight formula_weight	1841.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

KSQRQRSTSTPNVHM

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1a37a_
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	d1a37b_
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 (2 domains)

Domain ID domain_id	1a37A00
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	1a37B00
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 (2)

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Unit-cell length a length_a	94.730 Å
Unit-cell length b length_b	94.730 Å
Unit-cell length c length_c	250.870 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	3.600 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.3200
R_work r_work	0.3200
R_free r_free	0.3600

fit	/app/data/saxs_computation/a3/1a37/1a37.fit
pddf	/app/data/pr_computation/a3/1a37/1a37.pr.out
profile	/app/data/saxs_computation/a3/1a37/1a37.dat

14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)