SAXSdb — 1ej5

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

WISKOTT-ALDRICH SYNDROME PROTEIN

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 242–310 Chain A； UniProt 461–492	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 6.5；298 K；Ionic strength (raw mmCIF value) 75mM；Pressure ambient NMR measurement conditions：pH 6.5；298 K；Ionic strength (raw mmCIF value) 75mM；Pressure ambient NMR measurement conditions：pH 6.5；298 K；Ionic strength (raw mmCIF value) 75mM；Pressure ambient NMR measurement conditions：pH 6.5；298 K；Ionic strength (raw mmCIF value) 75mM；Pressure ambient NMR sample composition：1.6 mM protein U-15N; 25 mM phosphate buffer pH 6.5, 50 mM NaCl, 1 mM EDTA, 2 mM DTT \| 90% H2O/10% D2O NMR sample composition：1.6 mM protein U-15N,13C; 25 mM phosphate buffer pH 6.5, 50 mM NaCl, 1 mM EDTA, 2 mM DTT \| 90% H2O/10% D2O NMR sample composition：1.6 mM protein U-15N, 10% 13C; 25 mM phosphate buffer pH 6.5, 50 mM NaCl, 1 mM EDTA, 2 mM DTT \| 90% H2O/10% D2O NMR sample composition：1.6 mM protein U-15N,13C; 25 mM phosphate buffer pH 6.5, 50 mM NaCl, 1 mM EDTA, 2 mM DTT \| 100% D2O	Resolution not provided

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 1EJ5	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CEE SOLUTION STRUCTURE OF CDC42 IN COMPLEX WITH THE GTPASE BINDING DOMAIN OF WASP Deposited 1999-03-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 230–288（59 aa） Fragment：GTPASE BINDING DOMAIN OF WASP	Not recorded	MG MAGNESIUM ION × 1 GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 50mM；Pressure 1	Resolution not provided
1T84 Solution structure of the Wiskott-Aldrich Syndrome Protein (WASP) autoinhibited core domain complexed with (S)-wiskostatin, a small molecule inhibitor Deposited 2004-05-11	Different construct Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 242–310（69 aa） Fragment：core autoinhibited domain (GTPase binding domain is covalently linked to the cofilin homology and acidic regions) Chain A 361–492（132 aa） Fragment：core autoinhibited domain (GTPase binding domain is covalently linked to the cofilin homology and acidic regions)	Not recorded	WSK (2S)-1-(3,6-DIBROMO-9H-CARBAZOL-9-YL)-3-(DIMETHYLAMINO)PROPAN-2-OL × 1	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 20mM；Pressure ambient NMR sample composition 1mM WASP U-15N,13C; 1mM (S)-wiskostatin \| 20 mM Acetate-d3 pH 5.0; 20mM NaCl; 1mM DTT-d10; 5% DMSO-d6; 90% H2O/10% D2O or 100% D2O	Resolution not provided
2K42 Solution Structure of the GTPase Binding Domain of WASP in Complex with EspFU, an EHEC Effector Deposited 2008-05-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 242–310（69 aa） Fragment：CRIB domain, UNP residues 242-310	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；298.15 K；Pressure ambient NMR sample composition 1~1.5 mM [U-100% 13C; U-100% 15N] GBD/R33 complex, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1~1.5 mM [U-100% 13C; U-100% 15N] GBD/R33 complex, 100% D2O \| 100% D2O	Resolution not provided
2OT0 Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with a C-terminal peptide of Wiskott-Aldrich syndrome protein Deposited 2007-02-07	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 488–502（15 aa） Chain F 488–502（15 aa） Chain G 488–502（15 aa） Chain H 488–502（15 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；HEPES, MgCl2, PEG 550 MME, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.05 Å R-free 0.200

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

View Construct and Data Evidence

UniProt name	WASP_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–69； UniProt 242–310 Author chain A； PDBConstruct 76–107； UniProt 461–492

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	1ej5
Deposition date deposition_date	2000-02-29
Structure title title	SOLUTION STRUCTURE OF THE AUTOINHIBITED CONFORMATION OF WASP
Keywords keywords	alpha helix, beta-hairpin turn, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	16.15 Å
Radius of gyration Rg (electron density) rg_electron	15.26 Å
Forward intensity I(0) i0	927523000.00
Molecular weight molecular_weight	231650.0 kDa
Excluded volume excluded_volume	279860 Å³
Envelope volume envelope_volume	64440 Å³
Hydration-shell volume shell_volume	24780 Å³
Envelope diameter envelope_diameter	90.1 Å
Shell Rg shell_rg	28.83 Å
Envelope Rg envelope_rg	22.27 Å
Shape Rg shape_rg	15.27 Å
Total Rg total_rg	15.63 Å
Total atoms total_atoms	31640
Residues n_residues	2140
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	43.5 Å
Rg (real space) rg_real	15.12 Å
Rg uncertainty (real space) rg_real_error	0.07 Å
I(0) (real space) i0_real	8.8030e+08
I(0) uncertainty (real space) i0_real_error	8.1420e+06
Rg (reciprocal space) rg_reciprocal	16.29 Å
I(0) (reciprocal space) i0_reciprocal	927500000.0000
Solution quality estimate total_estimate	0.6774
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	18.2 Å
Skewness Skewness skewness	0.351
Kurtosis Kurtosis kurtosis	-0.263
Angular range angular_range	— – 0.4950 Å⁻¹
Current regularization parameter α current_alpha	3.0690
Highest regularization parameter α highest_alpha	2690000.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.012; Oscil: 0.949; Stabil: 0.988; Sysdev: 0.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

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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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1ej5a_
Class class	a — All alpha proteins
Fold Fold fold	a.68 — Wiscott-Aldrich syndrome protein, WASP, C-terminal domain
Superfamily Superfamily superfamily	a.68.1 — Wiscott-Aldrich syndrome protein, WASP, C-terminal domain
Family Family family	a.68.1.1 — Wiscott-Aldrich syndrome protein, WASP, C-terminal domain

CATH v4.4 (1 domains)

Domain ID domain_id	1ej5A00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	810 — SerineThreonine-protein kinase PAK-alpha; Chain A
Homologous superfamily homologous superfamily	10 — CRIB domain

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

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

Description description	WISKOTT-ALDRICH SYNDROME PROTEIN
Molecular weight formula_weight	11603.6 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	31640

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 BL21(DE3)

SOLUTION STRUCTURE OF THE AUTOINHIBITED CONFORMATION OF WASP

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

WISKOTT-ALDRICH SYNDROME PROTEIN

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

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)

fit	/app/data/saxs_computation/ej/1ej5/1ej5.fit
pddf	/app/data/pr_computation/ej/1ej5/1ej5.pr.out
profile	/app/data/saxs_computation/ej/1ej5/1ej5.dat