4hrl

Structural Basis for Eliciting a Cytotoxic Effect in HER2-Overexpressing Cancer Cells via Binding to the Extracellular Domain of HER2

Method: X-RAY DIFFRACTION D_max: 78.4 Å Quality: REASONABLE

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

Receptor tyrosine-protein kinase erbB-2

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 24–219	Fragment：N-terminal extracellular domain I, UNP RESIDUES 24-219 Mutation：N46D, N102D, N165D	Designed Ankyrin Repeat Protein 9_29 × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 5.6；293 K；0.2M ammonium acetate, 0.1M sodium citrate, 30% PEG 4000, pH 5.6, vapor diffusion, temperature 293K	Resolution 2.55 Å R-free 0.253

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 4HRL	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1MW4 Solution structure of the human Grb7-SH2 domain in complex with a 10 amino acid peptide pY1139 Deposited 2002-09-27	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1135–1144（10 aa） Fragment：SH2 domain binding site	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.6；298 K；Ionic strength (raw mmCIF value) 100 mM NaCl；Pressure 1 NMR sample composition 0.7mM Grb7 SH2 U-15N, 13C, 50mM acetate \| 90% H2O/10% D2O	Resolution not provided
1N8Z Crystal structure of extracellular domain of human HER2 complexed with Herceptin Fab Deposited 2002-11-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 23–629（607 aa） Fragment：extracellular domain	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；20-30% PEG 5000 MME, 0.1M MES pH6.5, 0.2M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.52 Å R-free 0.284
1QR1 POOR BINDING OF A HER-2/NEU EPITOPE (GP2) TO HLA-A2.1 IS DUE TO A LACK OF INTERACTIONS IN THE CENTER OF THE PEPTIDE Deposited 1999-06-17	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 654–662（9 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；295 K；14% PEG 6000, 25 mM MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 22K	Resolution 2.40 Å R-free 0.284
1QR1 POOR BINDING OF A HER-2/NEU EPITOPE (GP2) TO HLA-A2.1 IS DUE TO A LACK OF INTERACTIONS IN THE CENTER OF THE PEPTIDE Deposited 1999-06-17	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 654–662（9 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；295 K；14% PEG 6000, 25 mM MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 22K	Resolution 2.40 Å R-free 0.284
1S78 Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex Deposited 2004-01-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 23–646（624 aa） Fragment：extracellular domain (residues 23-646)	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；PEG 3350, ammonium formate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.25 Å R-free 0.268
1S78 Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex Deposited 2004-01-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 23–646（624 aa） Fragment：extracellular domain (residues 23-646)	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；PEG 3350, ammonium formate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.25 Å R-free 0.268
2A91 Crystal structure of ErbB2 domains 1-3 Deposited 2005-07-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 22–530（509 aa） Fragment：residues 1-510 + FLAG peptide	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；291 K；PEG 1500, glycerol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.50 Å R-free 0.264
2JWA ErbB2 transmembrane segment dimer spatial structure Deposited 2007-10-09	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 641–684（44 aa） Fragment：UNP residues 641-684 Chain B 641–684（44 aa） Fragment：UNP residues 641-684	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；313 K；Pressure ambient NMR sample composition 2.0mM [U-15N] ErbB2, 64mM [U-2H] DHPC, 16mM [U-2H] DMPC, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 2.0mM [U-13C; U-15N] ErbB2, 64mM [U-2H] DHPC, 16mM [U-2H] DMPC, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 1.0mM [U-13C; U-15N] ErbB2, 64mM [U-2H] DHPC, 16mM [U-2H] DMPC, 1.0mM ErbB2, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
2KS1 Heterodimeric association of Transmembrane domains of ErbB1 and ErbB2 receptors Enabling Kinase Activation Deposited 2009-12-24	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 641–684（44 aa） Fragment：ErbB2TM domain, UNP residues 641-684	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.5；313 K；Ionic strength (raw mmCIF value) 10；Pressure ambient NMR sample composition 1 mM [U-100% 15N] ErbB1TM-1, 1 mM [U-100% 15N] ErbB2TM-2, 12 mM DMPC-3, 48 mM DHPC-4, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 1 mM [U-100% 13C; U-100% 15N] ErbB1TM-5, 1 mM ErbB2TM-6, 12 mM [U-2H] DMPC-7, 48 mM [U-2H] DHPC-8, 100% D2O \| 100% D2O NMR sample composition 1 mM ErbB1TM-9, 1 mM [U-100% 13C; U-100% 15N] ErbB2TM-10, 12 mM [U-2H] DMPC-11, 48 mM [U-2H] DHPC-12, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 1 mM [U-100% 13C; U-100% 15N] ErbB1TM-13, 1 mM ErbB2TM-14, 12 mM [U-2H] DMPC-15, 48 mM [U-2H] DHPC-16, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
2L4K Water refined solution structure of the human Grb7-SH2 domain in complex with the 10 amino acid peptide pY1139 Deposited 2010-10-07	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1135–1144（10 aa） Fragment：unp residues 1135-1144	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.6；298 K；Pressure ambient NMR sample composition 0.6-0.8 mM [U-100% 13C; U-100% 15N] Grb7-SH2 domain-1, 0.6-0.8 mM [U-100% 13C; U-100% 15N] pY1139 peptide-2, 52.2 mM acetic acid-3, 100 mM sodium chloride-4, 5 mM DTT-5, 1 mM EDTA-6, 0.9 mM sodium azide-7, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2N2A Spatial structure of HER2/ErbB2 dimeric transmembrane domain in the presence of cytoplasmic juxtamembrane domains Deposited 2015-05-05	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 644–700（57 aa） Fragment：transmembrane domain (UNP residues 644-700) Chain B 644–700（57 aa） Fragment：transmembrane domain (UNP residues 644-700)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.5；318 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient NMR sample composition 4 mM [U-100% 2H] DPC, 1 mM [U-100% 13C; U-100% 15N] labeled protein, 1 mM unlabeled protein, 50 mM sodium acetate, 0.1 % sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 4 mM [U-100% 2H] DPC, 1 mM [U-100% 13C; U-100% 15N] labeled protein, 50 mM sodium acetate, 0.1 % sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 4 mM [U-100% 2H] DPC, 1 mM [U-100% 13C; U-100% 15N] labeled protein, 50 mM sodium acetate, 0.1 % sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
3BE1 Dual specific bH1 Fab in complex with the extracellular domain of HER2/ErbB-2 Deposited 2007-11-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 23–646（624 aa） Fragment：sequence database residues 23-646	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；292 K；Crystals of the Fab/HER2 complex were obtained by mixing protein solution (11 mg/ml protein, 25 mM Tris-HCl pH 8 and 150 mM sodium chloride) with crystallization buffer containing 25% w/v PEG2000, 0.1M MES pH 6.5. Before data collection the crystals were flash frozen in liquid nitrogen with 20% Ethylene Glycol as cryo-protectant, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.90 Å R-free 0.277
3H3B Crystal structure of the single-chain Fv (scFv) fragment of an anti-ErbB2 antibody chA21 in complex with residues 1-192 of ErbB2 extracellular domain Deposited 2009-04-16	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 23–214（192 aa） Fragment：extracellular domain, UNP residues 23-214	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；295 K；15% polyethylene glycol 4000, 100mM 3-(1-pyridino)-1-propane sulfonate, 100mM Na cacodylate pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.45 Å R-free 0.255
3H3B Crystal structure of the single-chain Fv (scFv) fragment of an anti-ErbB2 antibody chA21 in complex with residues 1-192 of ErbB2 extracellular domain Deposited 2009-04-16	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 23–214（192 aa） Fragment：extracellular domain, UNP residues 23-214	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；295 K；15% polyethylene glycol 4000, 100mM 3-(1-pyridino)-1-propane sulfonate, 100mM Na cacodylate pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.45 Å R-free 0.255
3MZW HER2 extracelluar region with affinity matured 3-helix affibody ZHER2:342 Deposited 2010-05-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 23–646（624 aa） Fragment：Extracellular domain residues 23-646	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；279 K；0.05M sodium chloride, 7.5% PEG3350, 0.1M ammonium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 2.90 Å R-free 0.278
3N85 Crystallographic trimer of HER2 extracellular regions in complex with tryptophan-rich antibody fragment Deposited 2010-05-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 23–646（624 aa） Fragment：UNP residues 23-646	Not recorded	CL CHLORIDE ION × 3 SO4 SULFATE ION × 48	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.3；293 K；NaCl, Na/K-phosphate, Li-sulfate, pH 7.3, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 3.20 Å R-free 0.230
3PP0 Crystal Structure of the Kinase domain of Human HER2 (erbB2). Deposited 2010-11-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 706–1009（304 aa） Fragment：kinase domain, residues 706-1009	Mutation：M706A, Q711L, M712L	03Q 2-{2-[4-({5-chloro-6-[3-(trifluoromethyl)phenoxy]pyridin-3-yl}amino)-5H-pyrrolo[3,2-d]pyrimidin-5-yl]ethoxy}ethanol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；20% PEG 3550, 200mM di-Ammonium Tartrate, 100 mM PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K	Resolution 2.25 Å R-free 0.260
3PP0 Crystal Structure of the Kinase domain of Human HER2 (erbB2). Deposited 2010-11-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 706–1009（304 aa） Fragment：kinase domain, residues 706-1009	Mutation：M706A, Q711L, M712L	03Q 2-{2-[4-({5-chloro-6-[3-(trifluoromethyl)phenoxy]pyridin-3-yl}amino)-5H-pyrrolo[3,2-d]pyrimidin-5-yl]ethoxy}ethanol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；20% PEG 3550, 200mM di-Ammonium Tartrate, 100 mM PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K	Resolution 2.25 Å R-free 0.260
3RCD HER2 Kinase Domain Complexed with TAK-285 Deposited 2011-03-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 713–1028（316 aa） Fragment：UNP residues 713-1028	Not recorded	03P N-{2-[4-({3-chloro-4-[3-(trifluoromethyl)phenoxy]phenyl}amino)-5H-pyrrolo[3,2-d]pyrimidin-5-yl]ethyl}-3-hydroxy-3-methylbutanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；20% PEG 3550, 200MM DI-AMMONIUM TARTRATE, 100 MM PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.21 Å R-free 0.294
3RCD HER2 Kinase Domain Complexed with TAK-285 Deposited 2011-03-30	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 713–1028（316 aa） Fragment：UNP residues 713-1028	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；20% PEG 3550, 200MM DI-AMMONIUM TARTRATE, 100 MM PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.21 Å R-free 0.294
3RCD HER2 Kinase Domain Complexed with TAK-285 Deposited 2011-03-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 713–1028（316 aa） Fragment：UNP residues 713-1028	Not recorded	03P N-{2-[4-({3-chloro-4-[3-(trifluoromethyl)phenoxy]phenyl}amino)-5H-pyrrolo[3,2-d]pyrimidin-5-yl]ethyl}-3-hydroxy-3-methylbutanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；20% PEG 3550, 200MM DI-AMMONIUM TARTRATE, 100 MM PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.21 Å R-free 0.294
3RCD HER2 Kinase Domain Complexed with TAK-285 Deposited 2011-03-30	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 713–1028（316 aa） Fragment：UNP residues 713-1028	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；20% PEG 3550, 200MM DI-AMMONIUM TARTRATE, 100 MM PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.21 Å R-free 0.294
3RCD HER2 Kinase Domain Complexed with TAK-285 Deposited 2011-03-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 713–1028（316 aa） Fragment：UNP residues 713-1028 Chain B 713–1028（316 aa） Fragment：UNP residues 713-1028	Not recorded	03P N-{2-[4-({3-chloro-4-[3-(trifluoromethyl)phenoxy]phenyl}amino)-5H-pyrrolo[3,2-d]pyrimidin-5-yl]ethyl}-3-hydroxy-3-methylbutanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；20% PEG 3550, 200MM DI-AMMONIUM TARTRATE, 100 MM PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.21 Å R-free 0.294
3RCD HER2 Kinase Domain Complexed with TAK-285 Deposited 2011-03-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 713–1028（316 aa） Fragment：UNP residues 713-1028 Chain D 713–1028（316 aa） Fragment：UNP residues 713-1028	Not recorded	03P N-{2-[4-({3-chloro-4-[3-(trifluoromethyl)phenoxy]phenyl}amino)-5H-pyrrolo[3,2-d]pyrimidin-5-yl]ethyl}-3-hydroxy-3-methylbutanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；20% PEG 3550, 200MM DI-AMMONIUM TARTRATE, 100 MM PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.21 Å R-free 0.294
3WLW Molecular Architecture of the ErbB2 Extracellular Domain Homodimer Deposited 2013-11-15	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 23–586（564 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.7；291 K；0.1M Ammonium acetate, 0.1M BIS-TRIS pH 5.7, 13% w/v Polyethylene glycol 10000, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K	Resolution 3.09 Å R-free 0.269
3WLW Molecular Architecture of the ErbB2 Extracellular Domain Homodimer Deposited 2013-11-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 23–586（564 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.7；291 K；0.1M Ammonium acetate, 0.1M BIS-TRIS pH 5.7, 13% w/v Polyethylene glycol 10000, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K	Resolution 3.09 Å R-free 0.269
3WSQ Structure of HER2 with an Fab Deposited 2014-03-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 23–586（564 aa） Fragment：UNP residues 23-586	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；1.1M sodium malonate pH 7.0, 0.1M HEPES 7.0, 0.5% v/v Jeffamine ED-2001, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 3.50 Å R-free 0.258
4HRM Structural Basis for Eliciting a Cytotoxic Effect in HER2-Overexpressing Cancer Cells via Binding to the Extracellular Domain of HER2 Deposited 2012-10-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 24–219（196 aa） Fragment：N-terminal extracellular domain I, UNP RESIDUES 24-219 Chain C 24–219（196 aa） Fragment：N-terminal extracellular domain I, UNP RESIDUES 24-219	Mutation：N46D, N102D, N165D Mutation：N46D, N102D, N165D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4.2；293 K；0.2 M sodium chloride, 0.1 M phosphate citrate, 20% PEG 8000, pH 4.2, vapor diffusion, temperature 293K	Resolution 3.20 Å R-free 0.339
4HRN Structural Basis for Eliciting a Cytotoxic Effect in HER2-Overexpressing Cancer Cells via Binding to the Extracellular Domain of HER2 Deposited 2012-10-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 529–625（97 aa） Fragment：Domain IV, UNP RESIDUES 529-625 Chain D 529–625（97 aa） Fragment：Domain IV, UNP RESIDUES 529-625	Mutation：N8D, N49D Mutation：N8D, N49D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4；293 K；0.05M succinic acid, 29% ammonium sulfate, pH 4.0, vapor diffusion, temperature 293K	Resolution 2.65 Å R-free 0.249
4HRN Structural Basis for Eliciting a Cytotoxic Effect in HER2-Overexpressing Cancer Cells via Binding to the Extracellular Domain of HER2 Deposited 2012-10-28	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 529–625（97 aa） Fragment：Domain IV, UNP RESIDUES 529-625	Mutation：N8D, N49D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4；293 K；0.05M succinic acid, 29% ammonium sulfate, pH 4.0, vapor diffusion, temperature 293K	Resolution 2.65 Å R-free 0.249
4HRN Structural Basis for Eliciting a Cytotoxic Effect in HER2-Overexpressing Cancer Cells via Binding to the Extracellular Domain of HER2 Deposited 2012-10-28	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 529–625（97 aa） Fragment：Domain IV, UNP RESIDUES 529-625	Mutation：N8D, N49D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4；293 K；0.05M succinic acid, 29% ammonium sulfate, pH 4.0, vapor diffusion, temperature 293K	Resolution 2.65 Å R-free 0.249
4NND Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites Deposited 2013-11-17	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1109–1114（6 aa） Fragment：phosphorylated peptide (UNP residues 1109-1114)	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；293 K；0.1 M HEPES, 25% PEG3350, 6% Jeffamine M-600, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.291
4NND Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites Deposited 2013-11-17	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1109–1114（6 aa） Fragment：phosphorylated peptide (UNP residues 1109-1114)	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；293 K；0.1 M HEPES, 25% PEG3350, 6% Jeffamine M-600, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.291
4NND Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites Deposited 2013-11-17	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1109–1114（6 aa） Fragment：phosphorylated peptide (UNP residues 1109-1114)	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；293 K；0.1 M HEPES, 25% PEG3350, 6% Jeffamine M-600, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.291
4NND Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites Deposited 2013-11-17	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 1109–1114（6 aa） Fragment：phosphorylated peptide (UNP residues 1109-1114)	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；293 K；0.1 M HEPES, 25% PEG3350, 6% Jeffamine M-600, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.291
5K33 Crystal structure of extracellular domain of HER2 in complex with Fcab STAB19 Deposited 2016-05-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 23–629（607 aa）	Not recorded	GOL GLYCEROL × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；295 K；0.05 M MES, 10% w/v PEG3350	Resolution 3.30 Å R-free 0.271
5KWG Crystal structure of extracellular domain of HER2 in complex with Fcab H10-03-6 Deposited 2016-07-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 23–653（631 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；295 K；50 mM Citric acid, 18% (w/v) PEG 3350	Resolution 4.30 Å R-free 0.369
5MY6 Crystal structure of a HER2-Nb complex Deposited 2017-01-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 24–645（622 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.25；293.15 K；100 mM HEPES pH 7.25, 10% 2-propanol, 22% PEG 4000	Resolution 2.25 Å R-free 0.220
5O4G HER2 in complex with Fab MF3958 Deposited 2017-05-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 23–628（606 aa） Fragment：UNP residues 23-628	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；0.1 M MES pH 6.0, 15% PEG 6000	Resolution 3.00 Å R-free 0.271
5OB4 NMR spatial structure of HER2 TM domain dimer in DPC micelles. Deposited 2017-06-26	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 31–74（44 aa） Fragment：UNP residues 31-74 Chain B 31–74（44 aa） Fragment：UNP residues 31-74	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；313 K；Ionic strength (raw mmCIF value) 30；Pressure AMBIENT NMR sample composition 2.5 mM [U-100% 13C; U-100% 15N] HER2TM, 2.5 mM HER2TM, 200 mM [U-99% 2H] DPC, 20 mM potassium phosphate, 0.01 % sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6ATT 39S Fab bound to HER2 ecd Deposited 2017-08-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 23–652（630 aa） Fragment：UNP residues 23-652	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；295 K；PEG8000, ethylene glycol, MES buffer	Resolution 3.77 Å R-free 0.289
6BGT Structure of Trastuzumab Fab mutant in complex with Her2 extracellular domain Deposited 2017-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–652（652 aa） Fragment：UNP residues 1-652	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；293 K；100 mM MES, pH 6.5, 18% PEG3350, 10% glycerol	Resolution 2.70 Å R-free 0.247
6J71 HuA21-scFv in complex with the extracellular domain(ECD) of HER2 Deposited 2019-01-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 22–639（618 aa）	Not recorded	BMA beta-D-mannopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；289 K；0.1 M MES monohydrate pH 6.5, 12% (w/v) PEG 20,000	Resolution 2.92 Å R-free 0.267
6LBX Crystal structure of HER2 Domain IV and Rb-H2 Deposited 2019-11-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 531–626（96 aa） Fragment：Domain IV	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；290 K；0.1M Sodium Citrate/Citric Acid (pH 5.5), 20% PEG 3000	Resolution 2.03 Å R-free 0.228
6OGE Cryo-EM structure of Her2 extracellular domain-Trastuzumab Fab-Pertuzumab Fab complex Deposited 2019-04-02	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 × 5 PDB declaration: pentameric	Chain A 23–644（622 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.36 Å
7JXH HER2 in complex with JBJ-08-178-01 Deposited 2020-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 703–1024（322 aa） Fragment：kinase domain	Not recorded	VOY (2E)-N-[3-cyano-7-ethoxy-4-({3-methyl-4-[([1,2,4]triazolo[1,5-a]pyridin-7-yl)oxy]phenyl}amino)quinolin-6-yl]-4-(dimethylamino)but-2-enamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1 M PIPES pH 6.5, 0.3 M ammonium tartrate, 25% (w/v) PEG 3350	Resolution 3.27 Å R-free 0.285
7JXH HER2 in complex with JBJ-08-178-01 Deposited 2020-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 703–1024（322 aa） Fragment：kinase domain	Not recorded	VOY (2E)-N-[3-cyano-7-ethoxy-4-({3-methyl-4-[([1,2,4]triazolo[1,5-a]pyridin-7-yl)oxy]phenyl}amino)quinolin-6-yl]-4-(dimethylamino)but-2-enamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1 M PIPES pH 6.5, 0.3 M ammonium tartrate, 25% (w/v) PEG 3350	Resolution 3.27 Å R-free 0.285
7JXH HER2 in complex with JBJ-08-178-01 Deposited 2020-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 703–1024（322 aa） Fragment：kinase domain	Not recorded	VOY (2E)-N-[3-cyano-7-ethoxy-4-({3-methyl-4-[([1,2,4]triazolo[1,5-a]pyridin-7-yl)oxy]phenyl}amino)quinolin-6-yl]-4-(dimethylamino)but-2-enamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1 M PIPES pH 6.5, 0.3 M ammonium tartrate, 25% (w/v) PEG 3350	Resolution 3.27 Å R-free 0.285
7JXH HER2 in complex with JBJ-08-178-01 Deposited 2020-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 703–1024（322 aa） Fragment：kinase domain	Not recorded	VOY (2E)-N-[3-cyano-7-ethoxy-4-({3-methyl-4-[([1,2,4]triazolo[1,5-a]pyridin-7-yl)oxy]phenyl}amino)quinolin-6-yl]-4-(dimethylamino)but-2-enamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1 M PIPES pH 6.5, 0.3 M ammonium tartrate, 25% (w/v) PEG 3350	Resolution 3.27 Å R-free 0.285
7JXH HER2 in complex with JBJ-08-178-01 Deposited 2020-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain E 703–1024（322 aa） Fragment：kinase domain	Not recorded	VOY (2E)-N-[3-cyano-7-ethoxy-4-({3-methyl-4-[([1,2,4]triazolo[1,5-a]pyridin-7-yl)oxy]phenyl}amino)quinolin-6-yl]-4-(dimethylamino)but-2-enamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1 M PIPES pH 6.5, 0.3 M ammonium tartrate, 25% (w/v) PEG 3350	Resolution 3.27 Å R-free 0.285
7JXH HER2 in complex with JBJ-08-178-01 Deposited 2020-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain F 703–1024（322 aa） Fragment：kinase domain	Not recorded	VOY (2E)-N-[3-cyano-7-ethoxy-4-({3-methyl-4-[([1,2,4]triazolo[1,5-a]pyridin-7-yl)oxy]phenyl}amino)quinolin-6-yl]-4-(dimethylamino)but-2-enamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1 M PIPES pH 6.5, 0.3 M ammonium tartrate, 25% (w/v) PEG 3350	Resolution 3.27 Å R-free 0.285
7JXH HER2 in complex with JBJ-08-178-01 Deposited 2020-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 7 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain G 703–1024（322 aa） Fragment：kinase domain	Not recorded	VOY (2E)-N-[3-cyano-7-ethoxy-4-({3-methyl-4-[([1,2,4]triazolo[1,5-a]pyridin-7-yl)oxy]phenyl}amino)quinolin-6-yl]-4-(dimethylamino)but-2-enamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1 M PIPES pH 6.5, 0.3 M ammonium tartrate, 25% (w/v) PEG 3350	Resolution 3.27 Å R-free 0.285
7JXH HER2 in complex with JBJ-08-178-01 Deposited 2020-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 8 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain H 703–1024（322 aa） Fragment：kinase domain	Not recorded	VOY (2E)-N-[3-cyano-7-ethoxy-4-({3-methyl-4-[([1,2,4]triazolo[1,5-a]pyridin-7-yl)oxy]phenyl}amino)quinolin-6-yl]-4-(dimethylamino)but-2-enamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1 M PIPES pH 6.5, 0.3 M ammonium tartrate, 25% (w/v) PEG 3350	Resolution 3.27 Å R-free 0.285
7MN5 Structure of the HER2/HER3/NRG1b Heterodimer Extracellular Domain Deposited 2021-04-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–1029（1029 aa） Fragment：Extracellular Domain	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.93 Å
7MN6 Structure of the HER2 S310F/HER3/NRG1b Heterodimer Extracellular Domain Deposited 2021-04-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–1029（1029 aa） Fragment：Extracellular Domain	Mutation：S310F	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.09 Å
7MN8 Structure of the HER2/HER3/NRG1b Heterodimer Extracellular Domain bound to Trastuzumab Fab Deposited 2021-04-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–1029（1029 aa）	Mutation：S310F	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.45 Å
7PCD HER2 IN COMPLEX WITH A COVALENT INHIBITOR Deposited 2021-08-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 703–1029（327 aa） Fragment：NONE	Not recorded	70I 1-[4-[4-[[3,5-bis(chloranyl)-4-([1,2,4]triazolo[1,5-a]pyridin-7-yloxy)phenyl]amino]pyrimido[5,4-d]pyrimidin-6-yl]piperazin-1-yl]-4-(3-fluoranylazetidin-1-yl)butan-1-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.75；293 K；18% PEG3350, 50mM ammonium tartrate, 150mM sodium tartrate and 100mM BIS-TRIS	Resolution 1.77 Å R-free 0.241
7QVK NM-02 in complex with HER2-ECD Deposited 2022-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain AAA 23–646（624 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；13% PEG6000 (w/v), 0.1 M MES pH 6.5, 7% 2-methyl-2,4-pentanediol	Resolution 3.10 Å R-free 0.330
8FFJ Structure of Zanidatamab bound to HER2 Deposited 2022-12-08	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 X 23–644（622 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.50 Å
8HGO The EGF-bound EGFR/HER2 ectodomain complex 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 × 3 PDB declaration: trimeric	Chain B 1–693（693 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
8HGP The EREG-bound EGFR/HER2 ectodomain complex 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 × 3 PDB declaration: trimeric	Chain B 1–693（693 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.53 Å
8JYR Crystal structure of anti-HER2 antibody H2Mab-119 in complex with HER2 domain I Deposited 2023-07-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 23–216（194 aa） Fragment：domain I	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M Sodium citrate pH5.5, 20% w/v PEG3000	Resolution 1.69 Å R-free 0.209
8PWH Atomic structure and conformational variability of the HER2-Trastuzumab-Pertuzumab complex Deposited 2023-07-20	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 × 5 PDB declaration: pentameric	Chain E 23–646（624 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.17 Å
8Q6J Atomic structure and conformational variability of the HER2-Trastuzumab-Pertuzumab complex Deposited 2023-08-11	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 × 5 PDB declaration: pentameric	Chain E 23–646（624 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8U4K Structure of the HER2/HER4/BTC Heterodimer Extracellular Domain Deposited 2023-09-10	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 × 3 PDB declaration: trimeric	Chain B 24–629（606 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.27 Å
8U4L Structure of the HER2/HER4/NRG1b Heterodimer Extracellular Domain Deposited 2023-09-10	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 × 3 PDB declaration: trimeric	Chain B 24–629（606 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.31 Å
8U8X crystal structure of the receptor tyrosine kinase Human HER2 (ERBB2) YVMA mutant kinase domain in complex with inhibitor compound 27 Deposited 2023-09-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 694–1029（336 aa） Fragment：kinase domain	Mutation：YVMA inserted after residue 84	W9N 1-{(1R,3r,5S)-3-[(3M)-4-methyl-3-{3-methyl-4-[(1-methyl-1H-benzimidazol-5-yl)oxy]phenyl}-1H-pyrazolo[3,4-d]pyrimidin-1-yl]-8-azabicyclo[3.2.1]octan-8-yl}propan-1-one × 1 PEG DI(HYDROXYETHYL)ETHER × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；8% PEG 3350, 0.1M Tris pH8.5, 0.5M NaCl	Resolution 1.69 Å R-free 0.203
8VB5 Crystal structure of kinase domain of HER2 Exon 20 insertion mutant in complex with tucatinib Deposited 2023-12-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 703–1029（327 aa）	Not recorded	A1AAC Tucatinib × 1 EDO 1,2-ETHANEDIOL × 6 CL CHLORIDE ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 M Bicine pH 8.5, 11% w/v PEG 1500, 0.5mM Tucatinib	Resolution 1.48 Å R-free 0.187
8VQD HER2 S310F in complex with TL1 Fab Deposited 2024-01-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 23–652（630 aa）	Mutation：S310F	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；20mM Tris, 150mM NaCl, 0.7mM fluorinated octyl maltoside cryo-EM vitrification conditions Cryogen ETHANE；Vitrification carried out with blot force 5, blot time 4 s	Resolution 2.61 Å
8VQE Homodimeric structure of HER2 S310F extracellular region Deposited 2024-01-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 23–652（630 aa） Chain B 23–652（630 aa）	Mutation：S310F Mutation：S310F	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；20mM Tris, 150mM NaCl, 0.7mM Fluorinated octyl maltoside cryo-EM vitrification conditions Cryogen ETHANE；Vitrified	Resolution 2.67 Å
9IUT Crystal structure of cancer-specific anti-HER2 antibody H2Mab-250 in complex with epitope peptide Deposited 2024-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 611–618（8 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.2 M MgCl2, 0.1 M Bis-Tris pH 5.7, 25% w/v PEG 3350	Resolution 2.09 Å R-free 0.236
9IUT Crystal structure of cancer-specific anti-HER2 antibody H2Mab-250 in complex with epitope peptide Deposited 2024-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 611–618（8 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.2 M MgCl2, 0.1 M Bis-Tris pH 5.7, 25% w/v PEG 3350	Resolution 2.09 Å R-free 0.236
9L1S Structure of the HER2 (S310F) - pertuzumab (T30S/D31A) complex Deposited 2024-12-15	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 23–652（630 aa）	Mutation：S310F	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
9MTE CryoEM structure of extracellular domain of human HER2 complexed with two nano-bodies 27A05 and 47D05 Deposited 2025-01-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 23–652（630 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；50 mM Hepes pH7.5, 150 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE；BF4 Bt4	Resolution 2.66 Å
9MTX CryoEM structure of extracellular domain of human HER2 complexed with nano-bodies 29E09 Deposited 2025-01-12	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 23–652（630 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；50 mM Hepes pH7.5, 150 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.06 Å
9QBF HER2/ErbB2 extracellular domain (ECD) in compact conformation in complex with trastuzumab (TZB) antibody Deposited 2025-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 23–1029（1007 aa）	Mutation：Del1-22,Del1030-1255,C789S,C805S,C965S.	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
9QBG HER2/ErbB2 extracellular domain (ECD) in extended conformation in complex with trastuzumab (TZB) antibody Deposited 2025-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 23–1029（1007 aa）	Mutation：Del1-22,Del1030-1255,C789S,C805S,C965S.	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
9QBH HER2/ErbB2 extracellular domain (ECD) from a near full-length construct solubilized in amphipols. Deposited 2025-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 23–1029（1007 aa）	Mutation：Del1-22,Del1030-1255,C789S,C805S,C965S.	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.77 Å
9T3R Structure of human HER2 in complex with EPS232 Fab Deposited 2025-10-29	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 23–652（630 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9T3S Structure of human HER2 in complex with EPS226 Fab Deposited 2025-10-29	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 23–652（630 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å

57 other PDB entries and 80 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ERBB2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain C； PDBConstruct 2–197； UniProt 24–219

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	4hrl
Deposition date deposition_date	2012-10-28
Structure title title	Structural Basis for Eliciting a Cytotoxic Effect in HER2-Overexpressing Cancer Cells via Binding to the Extracellular Domain of HER2
Keywords keywords	TRANSFERASE-DE NOVO PROTEIN complex; TRANSFERASE/DE NOVO PROTEIN
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	23.24 Å
Radius of gyration Rg (electron density) rg_electron	22.42 Å
Forward intensity I(0) i0	23060600.00
Molecular weight molecular_weight	35735.0 kDa
Excluded volume excluded_volume	44364 Å³
Envelope volume envelope_volume	52813 Å³
Hydration-shell volume shell_volume	20537 Å³
Envelope diameter envelope_diameter	79.0 Å
Shell Rg shell_rg	28.22 Å
Envelope Rg envelope_rg	22.51 Å
Shape Rg shape_rg	22.40 Å
Total Rg total_rg	23.23 Å
Total atoms total_atoms	2517
Residues n_residues	331
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	78.4 Å
Rg (real space) rg_real	23.27 Å
Rg uncertainty (real space) rg_real_error	0.64 Å
I(0) (real space) i0_real	2.3060e+07
I(0) uncertainty (real space) i0_real_error	3.3220e+05
Rg (reciprocal space) rg_reciprocal	23.27 Å
I(0) (reciprocal space) i0_reciprocal	23060000.0000
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	24.1 Å
Skewness Skewness skewness	0.360
Kurtosis Kurtosis kurtosis	-0.401
Angular range angular_range	— – 0.3400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3194000.0000
Real-space data points n_real_points	66
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.853; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.949; Smooth: 0.948

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Receptor tyrosine-protein kinase erbB-2
Molecular weight formula_weight	22208.3 kDa
EC 编号 ec_number	2.7.10.1
Mutation mutation	N46D, N102D, N165D
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C
Atom count atom_count	2559

HQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTDASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLDNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTDRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVA

来源 Source

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	Spodoptera frugiperda

Entity 2 Entity 2 polymer

Description description	Designed Ankyrin Repeat Protein 9_29
Molecular weight formula_weight	18558.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A

MRGSHHHHHHGSDLGKKLLEAARAGQDDEVRILMANGADVNAHDFYGITPLHLAANFGHLEIVEVLLKHGADVNAFDYDNTPLHLAADAGHLEIVEVLLKYGADVNASDRDGHTPLHLAAREGHLEIVEVLLKNGADVNAQDKFGKTPFDLAIDNGNEDIAEVLQKAAKLN

来源 Source

来源生物 organism	synthetic
NCBI Class编号 ncbi_taxonomy_id	32630
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	31

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7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	4hrlA00
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	20 — Ankyrin repeat-containing domain

Domain ID domain_id	4hrlC00
Class class	3 — Alpha Beta
Architecture architecture	80 — Alpha-Beta Horseshoe
Topology topology	20 — 24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A
Homologous superfamily homologous superfamily	20 — Receptor L-domain

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8. Citations (1)

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Unit-cell length a length_a	46.600 Å
Unit-cell length b length_b	80.500 Å
Unit-cell length c length_c	115.100 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	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.550 Å
Low-resolution limit resolution_low	46.817 Å
R factor r_factor	0.2030
R_work r_work	0.2004
R_free r_free	0.2529

fit	/app/data/saxs_computation/hr/4hrl/4hrl.fit
pddf	/app/data/pr_computation/hr/4hrl/4hrl.pr.out
profile	/app/data/saxs_computation/hr/4hrl/4hrl.dat

Structural Basis for Eliciting a Cytotoxic Effect in HER2-Overexpressing Cancer Cells via Binding to the Extracellular Domain of HER2

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

Receptor tyrosine-protein kinase erbB-2

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)