SAXSdb — 1p9j

▼

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

chimera of Epidermal growth factor(EGF) and Transforming growth factor alpha (TGF-alpha)

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	Insufficient information Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 976–1022	Fragment：TGF-alpha (residues 1-7), EGF (residues 8-54)	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 6.3；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition：0.8mM T1E, 15N-labelled, 50mM phosphate buffer, 95% H20, 5%D20, pH 6.3, 20ug/mL pefabloc \| 95% H20, 5%D20, pH 6.3	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 1P9J	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1IVO Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains. Deposited 2002-03-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 971–1023（53 aa） Fragment：RESIDUES 1-53 Chain D 971–1023（53 aa） Fragment：RESIDUES 1-53	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.4；293 K；PEG4000, PEG6000, sodium acetate, sodium chloride, TRIS, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.30 Å R-free 0.326
1JL9 Crystal Structure of Human Epidermal Growth Factor Deposited 2001-07-16	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 971–1021（51 aa） Fragment：RESIDUES 1-51 Chain B 971–1021（51 aa） Fragment：RESIDUES 1-51	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.1；293 K；magnesium chloride, Bicine, CYMAL-3, sodium azide, pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.00 Å R-free 0.283
1NQL Structure of the extracellular domain of human epidermal growth factor (EGF) receptor in an inactive (low pH) complex with EGF. Deposited 2003-01-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 971–1023（53 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；297 K；PEG3400,ammonium sulfate, magnesium sulfate, sodium citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 297K	Resolution 2.80 Å R-free 0.310
7OM4 Nanobody EgB4 bound to the full extracellular EGFR-EGF complex Deposited 2021-05-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 971–1023（53 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 14	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M LiSO4, 0.1 M glycine pH 10.5, 1.1 M sodium dihydrogen phosphate and 0.72 M dipotassium hydrogen phosphate	Resolution 6.05 Å R-free 0.327
7SYD Cryo-EM structure of the extracellular module of the full-length EGFR bound to EGF "tips-juxtaposed" conformation Deposited 2021-11-24	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 971–1023（53 aa） Chain D 971–1023（53 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
7SYE Cryo-EM structure of the extracellular module of the full-length EGFR bound to EGF. "tips-separated" conformation Deposited 2021-11-24	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 971–1023（53 aa） Chain D 971–1023（53 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
7SZ0 Cryo-EM structure of the extracellular module of the full-length EGFR L834R bound to EGF. "tips-juxtaposed" conformation Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 971–1023（53 aa） Chain D 971–1023（53 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
7SZ1 Cryo-EM structure of the extracellular module of the full-length EGFR L834R bound to EGF. "tips-separated" conformation Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 971–1023（53 aa） Chain D 971–1023（53 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
8HGO The EGF-bound EGFR/HER2 ectodomain complex Deposited 2022-11-15	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 971–1023（53 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25mM Hepes, 150mM NaCl, 0.02%DDM-0.002%CHS cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.31 Å
8HGS The EGF-bound EGFR ectodomain homodimer Deposited 2022-11-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 971–1023（53 aa） Chain D 971–1023（53 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.81 Å

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	EGF_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 8–54； UniProt 976–1022

chimera of Epidermal growth factor(EGF) and Transforming growth factor alpha (TGF-alpha)

Homo sapiens

UniProt P01135

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 40–46	Fragment：TGF-alpha (residues 1-7), EGF (residues 8-54)	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 6.3；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition：0.8mM T1E, 15N-labelled, 50mM phosphate buffer, 95% H20, 5%D20, pH 6.3, 20ug/mL pefabloc \| 95% H20, 5%D20, pH 6.3	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 1P9J	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GK5 Solution Structure the mEGF/TGFalpha44-50 chimeric growth factor Deposited 2001-08-08	Different construct Different experimental conditions	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 83–89（7 aa） Fragment：UNP residues 977-1018,UNP residues 83-89	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3；298 K	Resolution not provided
1MOX Crystal Structure of Human Epidermal Growth Factor Receptor (residues 1-501) in complex with TGF-alpha Deposited 2002-09-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 40–89（50 aa） Chain D 40–89（50 aa）	Not recorded	PT PLATINUM (II) ION × 7 CD CADMIUM ION × 11 CL CHLORIDE ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；7% PEG 3350, 20% Trehalose, 10mM CdCl2, 100mM HEPES, di-mu-iodobis(ethylenediamine)diplatinum nitrate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.289
1YUF TYPE ALPHA TRANSFORMING GROWTH FACTOR, NMR, 16 MODELS WITHOUT ENERGY MINIMIZATION Deposited 1996-04-01	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 40–89（50 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1YUG TYPE ALPHA TRANSFORMING GROWTH FACTOR, NMR, 15 MODELS AFTER ECEPP/3 ENERGY MINIMIZATION Deposited 1996-04-01	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 40–89（50 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
2TGF THE SOLUTION STRUCTURE OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA Deposited 1991-01-23	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 40–89（50 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
3E50 Crystal structure of human insulin degrading enzyme in complex with transforming growth factor-alpha Deposited 2008-08-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 40–89（50 aa） Fragment：UNP residues 40-89, Transforming growth factor alpha chain	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.231
3E50 Crystal structure of human insulin degrading enzyme in complex with transforming growth factor-alpha Deposited 2008-08-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 40–89（50 aa） Fragment：UNP residues 40-89, Transforming growth factor alpha chain	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.231
3TGF THE SOLUTION STRUCTURE OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA Deposited 1991-01-23	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 40–89（50 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
4TGF SOLUTION STRUCTURES OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA DERIVED FROM 1*H NMR DATA Deposited 1990-06-13	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 40–89（50 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
5KN5 TGFalpha/Epiregulin complex with neutralizing antibody LY3016859 Deposited 2016-06-27	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 48–87（40 aa）	Not recorded	SO4 SULFATE ION × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；294 K；100mM MES pH 6, 14% PEG 3350, 200mM Sodium Sulfate	Resolution 2.80 Å R-free 0.263
5KN5 TGFalpha/Epiregulin complex with neutralizing antibody LY3016859 Deposited 2016-06-27	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 48–87（40 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；294 K；100mM MES pH 6, 14% PEG 3350, 200mM Sodium Sulfate	Resolution 2.80 Å R-free 0.263
7SZ5 Cryo-EM structure of the extracellular module of the full-length EGFR bound to TGF-alpha "tips-separated" conformation Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 40–89（50 aa） Chain D 40–89（50 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
7SZ7 Cryo-EM structure of the extracellular module of the full-length EGFR bound to TGF-alpha. "tips-juxtaposed" conformation Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 40–89（50 aa） Chain D 40–89（50 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

11 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TGFA_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–7； UniProt 40–46

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	1p9j
Deposition date deposition_date	2003-05-12
Structure title title	Solution structure and dynamics of the EGF/TGF-alpha chimera T1E
Keywords keywords	chimera, EGF, TGF-alpha, ErbB1, ErbB3, HORMONE-GROWTH FACTOR COMPLEX; HORMONE/GROWTH FACTOR
Experimental Method method	SOLUTION NMR

▼

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

Radius of gyration Rg (Guinier) rg_guinier	13.28 Å
Radius of gyration Rg (electron density) rg_electron	14.30 Å
Forward intensity I(0) i0	773281000.00
Molecular weight molecular_weight	227820.0 kDa
Excluded volume excluded_volume	280210 Å³
Envelope volume envelope_volume	19830 Å³
Hydration-shell volume shell_volume	11333 Å³
Envelope diameter envelope_diameter	55.3 Å
Shell Rg shell_rg	20.58 Å
Envelope Rg envelope_rg	16.24 Å
Shape Rg shape_rg	14.37 Å
Total Rg total_rg	14.17 Å
Total atoms total_atoms	30456
Residues n_residues	1944
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	44.7 Å
Rg (real space) rg_real	13.52 Å
Rg uncertainty (real space) rg_real_error	0.42 Å
I(0) (real space) i0_real	7.7330e+08
I(0) uncertainty (real space) i0_real_error	8.1630e+06
Rg (reciprocal space) rg_reciprocal	13.50 Å
I(0) (reciprocal space) i0_reciprocal	773300000.0000
Solution quality estimate total_estimate	0.7206
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	11.3 Å
Skewness Skewness skewness	0.621
Kurtosis Kurtosis kurtosis	-0.142
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	82160.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.640; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.454; Smooth: 0.000

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1p9ja_
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.11 — EGF/Laminin
Family Family family	g.3.11.1 — EGF-type module

CATH v4.4 (1 domains)

Domain ID domain_id	1p9jA00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	25 — Laminin
Homologous superfamily homologous superfamily	10 — Laminin

▶

8. Citations (1)

▶

Description description	chimera of Epidermal growth factor(EGF) and Transforming growth factor alpha (TGF-alpha)
Molecular weight formula_weight	6339.2 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	30456

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	Pichia pastoris

fit	/app/data/saxs_computation/p9/1p9j/1p9j.fit
pddf	/app/data/pr_computation/p9/1p9j/1p9j.pr.out
profile	/app/data/saxs_computation/p9/1p9j/1p9j.dat

Solution structure and dynamics of the EGF/TGF-alpha chimera T1E

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

chimera of Epidermal growth factor(EGF) and Transforming growth factor alpha (TGF-alpha)

State in the Current Structure

Other States of the Same Protein in the Database

chimera of Epidermal growth factor(EGF) and Transforming growth factor alpha (TGF-alpha)

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

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)