SAXSdb — 1eyh

▼

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

EPSIN

Rattus norvegicus

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 15–158	Fragment：ENTH DOMAIN	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；30% PEG 4000, 100mM Tris-HCl pH 8.5, 0.2M MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 20K	Resolution 1.56 Å R-free 0.226

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 1EYH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1EDU CRYSTAL STRUCTURE OF THE ENTH DOMAIN OF RAT EPSIN 1 Deposited 2000-01-28	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 12–160（149 aa） Fragment：N-TERMINAL FRAGMENT	Non-standard monomer：Yes (specific site not provided by mmCIF)	EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG 4000, Na-HEPES, ethylene glycol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 20K	Resolution 1.80 Å R-free 0.224
1H0A Epsin ENTH bound to Ins(1,4,5)P3 Deposited 2002-06-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–158（158 aa） Fragment：ENTH DOMAIN, RESIDUES 1-158	Not recorded	DIO 1,4-DIETHYLENE DIOXIDE × 5 I3P D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；35-38% DIOXANE, pH 7.40	Resolution 1.70 Å R-free 0.228
1KY6 AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE Deposited 2002-02-03	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain P 375–381（7 aa） Fragment：RESIDUES 375-381	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å R-free 0.245

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

View Construct and Data Evidence

UniProt name	EPN1_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–144； UniProt 15–158

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1eyh
Deposition date deposition_date	2000-05-06
Structure title title	CRYSTAL STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN AT 1.56 ANGSTROM RESOLUTION
Keywords keywords	SUPERHELIX OF HELICES, CELL CYCLE; CELL CYCLE
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	16.72 Å
Radius of gyration Rg (electron density) rg_electron	15.36 Å
Forward intensity I(0) i0	5817020.00
Molecular weight molecular_weight	16754.0 kDa
Excluded volume excluded_volume	20751 Å³
Envelope volume envelope_volume	24317 Å³
Hydration-shell volume shell_volume	13477 Å³
Envelope diameter envelope_diameter	55.4 Å
Shell Rg shell_rg	21.11 Å
Envelope Rg envelope_rg	15.94 Å
Shape Rg shape_rg	15.38 Å
Total Rg total_rg	16.37 Å
Total atoms total_atoms	1175
Residues n_residues	144
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

▼

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

Maximum dimension Dmax dmax	55.5 Å
Rg (real space) rg_real	16.65 Å
Rg uncertainty (real space) rg_real_error	0.31 Å
I(0) (real space) i0_real	5.8170e+06
I(0) uncertainty (real space) i0_real_error	7.1850e+04
Rg (reciprocal space) rg_reciprocal	16.66 Å
I(0) (reciprocal space) i0_reciprocal	5817000.0000
Solution quality estimate total_estimate	0.7144
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	21.6 Å
Skewness Skewness skewness	0.210
Kurtosis Kurtosis kurtosis	-0.357
Angular range angular_range	— – 0.4750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1302000.0000
Real-space data points n_real_points	78
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.822; Stabil: 1.000; Sysdev: 0.272; Positv: 1.000; Valcen: 0.999; Smooth: 0.999

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1eyha_
Class class	a — All alpha proteins
Fold Fold fold	a.118 — alpha-alpha superhelix
Superfamily Superfamily superfamily	a.118.9 — ENTH/VHS domain
Family Family family	a.118.9.1 — ENTH domain

CATH v4.4 (1 domains)

Domain ID domain_id	1eyhA00
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	90 —

▶

8. Citations (1)

▶

Unit-cell length a length_a	49.885 Å
Unit-cell length b length_b	49.885 Å
Unit-cell length c length_c	99.333 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	6

Space group space_group	P 31 2 1
Space-group number int_tables_number	152
Crystal system crystal_system	—

Resolution resolution	1.560 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2010
R_work r_work	0.1990
R_free r_free	0.2260

Description description	EPSIN
Molecular weight formula_weight	16780.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1386

CRYSTAL STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN AT 1.56 ANGSTROM RESOLUTION

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

EPSIN

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 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	195

fit	/app/data/saxs_computation/ey/1eyh/1eyh.fit
pddf	/app/data/pr_computation/ey/1eyh/1eyh.pr.out
profile	/app/data/saxs_computation/ey/1eyh/1eyh.dat