← Back to search
1gk5

Solution Structure the mEGF/TGFalpha44-50 chimeric growth factor

Method: SOLUTION NMR Dmax: 48.9 Å Quality: REASONABLE
▼

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

Pro-epidermal growth factor,Protransforming growth factor alpha

Homo sapiens

UniProt P01132

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 977–1018 Fragment：UNP residues 977-1018,UNP residues 83-89 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 3；298 K 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 1GK5 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1A3P ROLE OF THE 6-20 DISULFIDE BRIDGE IN THE STRUCTURE AND ACTIVITY OF EPIDERMAL GROWTH FACTOR, NMR, 20 STRUCTURES Deposited 1998-01-22 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 980–1024（45 aa） Fragment：RESIDUES 4 - 48
Mutation：DEL(1-3, 49-53), C6(AMINO-BUTYRIC ACID), C20 (AMINO-BUTYRIC ACID) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 2.8；300 K；Pressure 1
NMR sample composition H2O
Resolution not provided
1EGF SOLUTION STRUCTURE OF MURINE EPIDERMAL GROWTH FACTOR DETERMINED BY NMR SPECTROSCOPY AND REFINED BY ENERGY MINIMIZATION WITH RESTRAINTS Deposited 1991-10-01 Different construct Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 977–1029（53 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1EPG THREE-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE STRUCTURES OF MOUSE EPIDERMAL GROWTH FACTOR IN ACIDIC AND PHYSIOLOGICAL PH SOLUTIONS Deposited 1992-03-24 Different construct Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 977–1029（53 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1EPH THREE-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE STRUCTURES OF MOUSE EPIDERMAL GROWTH FACTOR IN ACIDIC AND PHYSIOLOGICAL PH SOLUTIONS Deposited 1992-03-24 Different construct Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 977–1029（53 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1EPI THREE-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE STRUCTURES OF MOUSE EPIDERMAL GROWTH FACTOR IN ACIDIC AND PHYSIOLOGICAL PH SOLUTIONS Deposited 1992-03-24 Different construct Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 977–1029（53 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1EPJ THREE-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE STRUCTURES OF MOUSE EPIDERMAL GROWTH FACTOR IN ACIDIC AND PHYSIOLOGICAL PH SOLUTIONS Deposited 1992-03-24 Different construct Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 977–1029（53 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
3EGF SOLUTION STRUCTURE OF MURINE EPIDERMAL GROWTH FACTOR DETERMINED BY NMR SPECTROSCOPY AND REFINED BY ENERGY MINIMIZATION WITH RESTRAINTS Deposited 1992-08-30 Different construct Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 977–1029（53 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EGF_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–42； UniProt 977–1018

Pro-epidermal growth factor,Protransforming growth factor 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 83–89 Fragment：UNP residues 977-1018,UNP residues 83-89 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 3；298 K 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 1GK5 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
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
1P9J Solution structure and dynamics of the EGF/TGF-alpha chimera T1E Deposited 2003-05-12 Different construct Different experimental conditions Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 40–46（7 aa） Fragment：TGF-alpha (residues 1-7), EGF (residues 8-54)
Not recorded No recorded non-water small molecule 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
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 43–49； UniProt 83–89

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1gk5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1gk5
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1gk5
Deposition date deposition_date2001-08-08
Structure title titleSolution Structure the mEGF/TGFalpha44-50 chimeric growth factor
Keywords keywordsGROWTH FACTOR, EGF GROWTH FACTOR, CHIMERIC; GROWTH FACTOR
Experimental Method methodSOLUTION NMR
▼

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

Radius of gyration Rg (Guinier) rg_guinier12.34 Å
Radius of gyration Rg (electron density) rg_electron12.74 Å
Forward intensity I(0) i051152100.00
Molecular weight molecular_weight52498.0 kDa
Excluded volume excluded_volume62684 ų
Envelope volume envelope_volume13558 ų
Hydration-shell volume shell_volume8734 ų
Envelope diameter envelope_diameter53.6 Å
Shell Rg shell_rg18.92 Å
Envelope Rg envelope_rg15.29 Å
Shape Rg shape_rg12.81 Å
Total Rg total_rg12.81 Å
Total atoms total_atoms6790
Residues n_residues490
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
▼

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

Maximum dimension Dmax dmax48.9 Å
Rg (real space) rg_real12.52 Å
Rg uncertainty (real space) rg_real_error0.61 Å
I(0) (real space) i0_real5.1150e+07
I(0) uncertainty (real space) i0_real_error6.8170e+05
Rg (reciprocal space) rg_reciprocal12.51 Å
I(0) (reciprocal space) i0_reciprocal51150000.0000
Solution quality estimate total_estimate0.6969
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary12.4 Å
Skewness Skewness skewness0.593
Kurtosis Kurtosis kurtosis0.083
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35830.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.597; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.265; 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_idd1gk5a_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.1 — EGF-type module

CATH v4.4 (1 domains)

Domain ID domain_id1gk5A00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin
▶

8. Citations (2)

▶

9. Files and Curves (10)