4qd2

Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex

Method: X-RAY DIFFRACTION D_max: 155.6 Å Quality: GOOD

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

Hemagglutinin component HA33

Clostridium botulinum

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 × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain C； UniProt 2–293 Chain D； UniProt 2–293	Not recorded	Hemagglutinin component HA17 × 1 （A5HZZ5） Hemagglutinin component HA70 × 1 （A5HZZ4） Cadherin-1 × 1 （P09803） CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Tris (pH8.0), 6% PEG8000, 200mM potassium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.40 Å R-free 0.247
2	Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain H； UniProt 2–293 Chain I； UniProt 2–293	Not recorded	Hemagglutinin component HA17 × 1 （A5HZZ5） Hemagglutinin component HA70 × 1 （A5HZZ4） Cadherin-1 × 1 （P09803） CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Tris (pH8.0), 6% PEG8000, 200mM potassium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.40 Å R-free 0.247

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	A5HZZ6_CLOBH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain C； PDBConstruct 1–292； UniProt 2–293 Author chain D； PDBConstruct 1–292； UniProt 2–293 Author chain H； PDBConstruct 1–292； UniProt 2–293 Author chain I； PDBConstruct 1–292； UniProt 2–293

Hemagglutinin component HA17

Clostridium botulinum

UniProt A5HZZ5

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 × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain B； UniProt 2–146	Not recorded	Hemagglutinin component HA33 × 2 （A5HZZ6） Hemagglutinin component HA70 × 1 （A5HZZ4） Cadherin-1 × 1 （P09803） CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Tris (pH8.0), 6% PEG8000, 200mM potassium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.40 Å R-free 0.247
2	Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain G； UniProt 2–146	Not recorded	Hemagglutinin component HA33 × 2 （A5HZZ6） Hemagglutinin component HA70 × 1 （A5HZZ4） Cadherin-1 × 1 （P09803） CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Tris (pH8.0), 6% PEG8000, 200mM potassium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.40 Å R-free 0.247

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	A5HZZ5_CLOBH
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 3–147； UniProt 2–146 Author chain G； PDBConstruct 3–147； UniProt 2–146

Hemagglutinin component HA70

Clostridium botulinum

UniProt A5HZZ4

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 × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain A； UniProt 378–626	Not recorded	Hemagglutinin component HA33 × 2 （A5HZZ6） Hemagglutinin component HA17 × 1 （A5HZZ5） Cadherin-1 × 1 （P09803） CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Tris (pH8.0), 6% PEG8000, 200mM potassium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.40 Å R-free 0.247
2	Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain F； UniProt 378–626	Not recorded	Hemagglutinin component HA33 × 2 （A5HZZ6） Hemagglutinin component HA17 × 1 （A5HZZ5） Cadherin-1 × 1 （P09803） CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Tris (pH8.0), 6% PEG8000, 200mM potassium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.40 Å R-free 0.247

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	A5HZZ4_CLOBH
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain A； PDBConstruct 6–254； UniProt 378–626 Author chain F； PDBConstruct 6–254； UniProt 378–626

Cadherin-1

Mus musculus

UniProt P09803

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 × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain E； UniProt 157–369	Not recorded	Hemagglutinin component HA33 × 2 （A5HZZ6） Hemagglutinin component HA17 × 1 （A5HZZ5） Hemagglutinin component HA70 × 1 （A5HZZ4） CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Tris (pH8.0), 6% PEG8000, 200mM potassium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.40 Å R-free 0.247
2	Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain J； UniProt 157–369	Not recorded	Hemagglutinin component HA33 × 2 （A5HZZ6） Hemagglutinin component HA17 × 1 （A5HZZ5） Hemagglutinin component HA70 × 1 （A5HZZ4） CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Tris (pH8.0), 6% PEG8000, 200mM potassium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.40 Å R-free 0.247

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 4QD2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1EDH E-CADHERIN DOMAINS 1 AND 2 IN COMPLEX WITH CALCIUM Deposited 1996-05-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 156–380（225 aa） Chain B 156–380（225 aa）	Mutation：INS(MR-D1) Mutation：INS(MR-D1)	HG MERCURY (II) ION × 2 CA CALCIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 9；1.2 M AMMONIUM SULFATE 0.01 M CALCIUM CHLORIDE 0.1 M TRIS-HCL BUFFER, PH 9.0 0.003 M SODIUM AZIDE	Resolution 2.00 Å R-free 0.262
1FF5 STRUCTURE OF E-CADHERIN DOUBLE DOMAIN Deposited 2000-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 157–374（218 aa） Fragment：DOUBLE DOMAIN Chain B 157–374（218 aa） Fragment：DOUBLE DOMAIN	Not recorded	CA CALCIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；50 mM ammonium sulfate, 50 mM NaOAc, 30% PEG 8000, pH 8.5, Tris-HCl, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.93 Å
1I7W BETA-CATENIN/PHOSPHORYLATED E-CADHERIN COMPLEX Deposited 2001-03-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 734–884（151 aa） Fragment：CYTOPLASMIC DOMAIN Chain D 734–884（151 aa） Fragment：CYTOPLASMIC DOMAIN	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 2 CL CHLORIDE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；polyethylene glycol monomethylether 5000, Tris-HCl, NaCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.245
1I7X BETA-CATENIN/E-CADHERIN COMPLEX Deposited 2001-03-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 734–884（151 aa） Fragment：CYTOPLASMIC DOMAIN Chain D 734–884（151 aa） Fragment：CYTOPLASMIC DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；POLYETHYLENEIMINE TRIS-HCL ISOPROPANOL, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.00 Å R-free 0.242
1Q1P E-Cadherin activation Deposited 2003-07-22	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 158–369（212 aa）	Not recorded	CA CALCIUM ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.20 Å R-free 0.305
1Q1P E-Cadherin activation Deposited 2003-07-22	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 158–369（212 aa）	Not recorded	CA CALCIUM ION × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.20 Å R-free 0.305
1SUH AMINO-TERMINAL DOMAIN OF EPITHELIAL CADHERIN IN THE CALCIUM BOUND STATE, NMR, 20 STRUCTURES Deposited 1996-01-30	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 156–300（145 aa） Fragment：AMINO-TERMINAL DOMAIN RESIDUES 1 - 104	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
2OMW Crystal structure of InlA S192N Y369S/mEC1 complex Deposited 2007-01-23	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 158–256（99 aa） Fragment：N-terminal domain of murine E-cadherin	Not recorded	CL CHLORIDE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；298 K；PEG 6000, LiCl, Na-Citrate, pH 5.2, vapor diffusion, hanging drop, temperature 298K	Resolution 1.85 Å R-free 0.207
2QVF mouse E-cadherin domains 1,2 Deposited 2007-08-08	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 157–369（213 aa） Fragment：Cadherin 1, Cadherin 2, UNP residues 157-369	Not recorded	CA CALCIUM ION × 8	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.40 Å R-free 0.286
3IFQ Interction of plakoglobin and beta-catenin with desmosomal cadherins Deposited 2009-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 778–884（107 aa） Fragment：residues 778-884 Chain D 778–884（107 aa） Fragment：residues 778-884	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289.5 K；17% PEG 3350, 0.1M Ammonium sulfate, 0.1M Tris-Cl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289.5K	Resolution 2.80 Å R-free 0.261
3IFQ Interction of plakoglobin and beta-catenin with desmosomal cadherins Deposited 2009-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 778–884（107 aa） Fragment：residues 778-884	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289.5 K；17% PEG 3350, 0.1M Ammonium sulfate, 0.1M Tris-Cl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289.5K	Resolution 2.80 Å R-free 0.261
3IFQ Interction of plakoglobin and beta-catenin with desmosomal cadherins Deposited 2009-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 778–884（107 aa） Fragment：residues 778-884	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289.5 K；17% PEG 3350, 0.1M Ammonium sulfate, 0.1M Tris-Cl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289.5K	Resolution 2.80 Å R-free 0.261
3LNE Crystal structure of E-cadherin EC12 K14E Deposited 2010-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 157–369（213 aa） Fragment：UNP residues 157-369	Mutation：K14E	CA CALCIUM ION × 6 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1M MES pH 6.5, 0.75M sodium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.219
3LNF Crystal structure of E-cadherin EC12 K14EW2A Deposited 2010-02-02	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 157–369（213 aa） Fragment：UNP residues 157-369	Mutation：K14E,W2A	CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；1.2M ammonium sulfate, 0.1M Tris-Cl pH 8.5, 15% (v/v) glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.241
3LNF Crystal structure of E-cadherin EC12 K14EW2A Deposited 2010-02-02	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 157–369（213 aa） Fragment：UNP residues 157-369	Mutation：K14E,W2A	CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；1.2M ammonium sulfate, 0.1M Tris-Cl pH 8.5, 15% (v/v) glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.241
3LNG Crystal structure of E-cadherin EC12 AA extension Deposited 2010-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 157–369（213 aa） Fragment：UNP residues 157-369 Chain B 157–369（213 aa） Fragment：UNP residues 157-369	Not recorded	CA CALCIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；293 K；0.1M Tris, pH 8.5, 1.3M ammonium sulfate, 15% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.70 Å R-free 0.263
3LNH Crystal structure of E-cadherin EC12 W2A Deposited 2010-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 157–369（213 aa） Fragment：UNP residues 157-369 Chain B 157–369（213 aa） Fragment：UNP residues 157-369	Mutation：W2A Mutation：W2A	CA CALCIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；293 K；0.1M Tris, pH 8.5, 1.3M ammonium sulfate, 15% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.60 Å R-free 0.267
3LNI Crystal structure of E-cadherin EC12 E89A Deposited 2010-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 157–369（213 aa） Fragment：UNP residues 157-369 Chain B 157–369（213 aa） Fragment：UNP residues 157-369	Mutation：E89A Mutation：E89A	CA CALCIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.25M ammonium sulfate, 0.1M MES pH 6.5, 26% PEG 5000 monomethylether, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.30 Å R-free 0.228
3Q2L Mouse E-cadherin EC1-2 V81D mutant Deposited 2010-12-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 157–369（213 aa） Fragment：E-cadherin EC1-2 fragment, residues 157-369 Chain B 157–369（213 aa） Fragment：E-cadherin EC1-2 fragment, residues 157-369	Mutation：V81D Mutation：V81D	CA CALCIUM ION × 8 1PE PENTAETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；10% (v/v) PEG 400, 0.1M sodium acetate pH4.6, 0.13M CaCl2, Cryoprotected by increasing PEG 400 to 30%, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.70 Å R-free 0.245
3Q2N Mouse E-cadherin EC1-2 L175D mutant Deposited 2010-12-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 157–369（213 aa） Fragment：E-cadherin EC1-2 fragment, residues 157-369 Chain B 157–369（213 aa） Fragment：E-cadherin EC1-2 fragment, residues 157-369	Mutation：L175D Mutation：L175D	CA CALCIUM ION × 8 PG4 TETRAETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；25% (v/v) PEG 400, 0.1M sodium acetate pH4.6, 0.15M CaCl2 and croprotected by increasing PEG 400 to 30%., VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.73 Å R-free 0.224
3Q2V Crystal structure of mouse E-cadherin ectodomain Deposited 2010-12-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 157–700（544 aa） Fragment：UNP residues 157-700 Chain B 157–700（544 aa） Fragment：UNP residues 157-700	Not recorded	CA CALCIUM ION × 24 MN MANGANESE (II) ION × 2 MAN alpha-D-mannopyranose × 18	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；293 K；11% (w/v) PEG 5000 monomethyl ether (MME), 0.1M Bicine pH 8.5, 10mM CaCl2, 30mM MnCl2, 2% (v/v) dioxane, 4% (v/v) 1-butanol , VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.40 Å R-free 0.293
3QRB crystal structure of E-cadherin EC1-2 P5A P6A Deposited 2011-02-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 157–369（213 aa） Fragment：Cadherin 1 and Cadherin 2 Domains, UNP residues 157-369	Mutation：P161A, P162A	CA CALCIUM ION × 6 EDO 1,2-ETHANEDIOL × 4 PGE TRIETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；10% PEG8000, 10% ethylene glycol, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.80 Å R-free 0.178
3QRB crystal structure of E-cadherin EC1-2 P5A P6A Deposited 2011-02-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 157–369（213 aa） Fragment：Cadherin 1 and Cadherin 2 Domains, UNP residues 157-369	Mutation：P161A, P162A	CA CALCIUM ION × 6 EDO 1,2-ETHANEDIOL × 4 PGE TRIETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；10% PEG8000, 10% ethylene glycol, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.80 Å R-free 0.178
7AR4 Crystal structure of beta-catenin in complex with cyclic peptide inhibitor Deposited 2020-10-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain PaP 783–798（16 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293.15 K；0.1 M HEPES, 4% PEG6000, 20 mM TRIS, 150 mM NaCl, 0.5 % Glycerol, 2 mM DTT	Resolution 2.60 Å R-free 0.242

19 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CADH1_MOUSE
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain E； PDBConstruct 1–213； UniProt 157–369 Author chain J； PDBConstruct 1–213； UniProt 157–369

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	4qd2
Deposition date deposition_date	2014-05-13
Structure title title	Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex
Keywords keywords	Oral Toxicity, Botulinum Neurotoxin, E-Cadherin, HA70, HA17, HA33, CELL ADHESION; CELL ADHESION
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	48.22 Å
Radius of gyration Rg (electron density) rg_electron	47.54 Å
Forward intensity I(0) i0	1006480000.00
Molecular weight molecular_weight	263370.0 kDa
Excluded volume excluded_volume	329260 Å³
Envelope volume envelope_volume	476150 Å³
Hydration-shell volume shell_volume	82387 Å³
Envelope diameter envelope_diameter	163.6 Å
Shell Rg shell_rg	53.17 Å
Envelope Rg envelope_rg	46.03 Å
Shape Rg shape_rg	47.54 Å
Total Rg total_rg	47.76 Å
Total atoms total_atoms	18610
Residues n_residues	2303
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	155.6 Å
Rg (real space) rg_real	47.95 Å
Rg uncertainty (real space) rg_real_error	1.46 Å
I(0) (real space) i0_real	1.0060e+09
I(0) uncertainty (real space) i0_real_error	1.9420e+07
Rg (reciprocal space) rg_reciprocal	48.21 Å
I(0) (reciprocal space) i0_reciprocal	1007000000.0000
Solution quality estimate total_estimate	0.8765
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	66.0 Å
Skewness Skewness skewness	0.153
Kurtosis Kurtosis kurtosis	-0.344
Angular range angular_range	— – 0.1650 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	68150000.0000
Real-space data points n_real_points	34
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.849; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.868

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5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Hemagglutinin component HA33
Molecular weight formula_weight	34081.7 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,C,I,H
Atom count atom_count	19012

EHYSVIQNSLNDKIVTISCKADTNLFFYQVAGNVSLFQQTRNYLERWRLIYDSNKAAYKIKSMDIHNTNLVLTWNAPTHNISTQQDSNADNQYWLLLKDIGNNSFIIASYKNPNLVLYADTVARNLKLSTLNNSNYIKFIIEDYIISDLNNFTCKISPILDLNKVVQQVDVTNLNVNLYTWDYGRNQKWTIRYNEEKAAYQFFNTILSNGVLTWIFSNGNTVRVSSSNDQNNDAQYWLINPVSDTDETYTITNLRDTTKALDLYGGQTANGTAIQVFNYHGDDNQKWNIRNPPGSA

来源 Source

来源生物 organism	Clostridium botulinum
NCBI Class编号 ncbi_taxonomy_id	441771
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Hemagglutinin component HA17
Molecular weight formula_weight	17069.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,G

GPSVERTFLPNGNYNIKSIFSGSLYLNPVSKSLTFSNESSANNQKWNVEYMAENRCFKISNVAEPNKYLSYDNFGFISLDSLSNRCYWFPIKIAVNTYIMLSLNKVNELDYAWDIYDTNENILSQPLLLLPNFDIYNSNQMFKLEKI

来源 Source

来源生物 organism	Clostridium botulinum
NCBI Class编号 ncbi_taxonomy_id	441771
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Hemagglutinin component HA70
Molecular weight formula_weight	28846.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,F

GPLGSPSENIQEINTAISDNYTYNIPGIVNNNPFYILFTVNTTGIYKINAQNNLPSLKIYEAIGSGNRNFQSGNLCDDDIKAINYITGFDSPNAKSYLVVLLNKDKNYYIRVPQTSSNIENQIQFKREEGDLRNLMNSSVNIIDNLNSTGAHYYTRQSPDVHDYISYEFTIPGNFNNKDTSNIRLYTSYNQGIGTLFRVTETIDGYNLINIQQNLHLLNNTNSIRLLNGAIYILKVEVTELNNYNIRLHIDITN

来源 Source

来源生物 organism	Clostridium botulinum
NCBI Class编号 ncbi_taxonomy_id	441771
宿主生物 host_organism	Escherichia coli

Entity 4 Entity 4 polymer

Description description	Cadherin-1
Molecular weight formula_weight	23260.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,J

DWVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQGADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAVSSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGAVPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKNMFTVNRDTGVISVLTSGLDRESYPTYTLVVQAADLQGEGLSTTAKAVITVKD

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 5 Entity 5 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	402

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7. Fold Classification (SCOP + CATH) 31 domains

SCOP 2.08 (15 domains)

Domain ID domain_id	d4qd2c1
Class class	b — All beta proteins
Fold Fold fold	b.42 — beta-Trefoil
Superfamily Superfamily superfamily	b.42.2 — Ricin B-like lectins
Family Family family	b.42.2.0 — automated matches

Domain ID domain_id	d4qd2c2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4qd2d1
Class class	b — All beta proteins
Fold Fold fold	b.42 — beta-Trefoil
Superfamily Superfamily superfamily	b.42.2 — Ricin B-like lectins
Family Family family	b.42.2.0 — automated matches

Domain ID domain_id	d4qd2d2
Class class	b — All beta proteins
Fold Fold fold	b.42 — beta-Trefoil
Superfamily Superfamily superfamily	b.42.2 — Ricin B-like lectins
Family Family family	b.42.2.0 — automated matches

Domain ID domain_id	d4qd2d3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4qd2e1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.6 — Cadherin-like
Family Family family	b.1.6.1 — Cadherin

Domain ID domain_id	d4qd2e2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.6 — Cadherin-like
Family Family family	b.1.6.1 — Cadherin

Domain ID domain_id	d4qd2h1
Class class	b — All beta proteins
Fold Fold fold	b.42 — beta-Trefoil
Superfamily Superfamily superfamily	b.42.2 — Ricin B-like lectins
Family Family family	b.42.2.0 — automated matches

Domain ID domain_id	d4qd2h2
Class class	b — All beta proteins
Fold Fold fold	b.42 — beta-Trefoil
Superfamily Superfamily superfamily	b.42.2 — Ricin B-like lectins
Family Family family	b.42.2.0 — automated matches

Domain ID domain_id	d4qd2h3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4qd2i1
Class class	b — All beta proteins
Fold Fold fold	b.42 — beta-Trefoil
Superfamily Superfamily superfamily	b.42.2 — Ricin B-like lectins
Family Family family	b.42.2.0 — automated matches

Domain ID domain_id	d4qd2i2
Class class	b — All beta proteins
Fold Fold fold	b.42 — beta-Trefoil
Superfamily Superfamily superfamily	b.42.2 — Ricin B-like lectins
Family Family family	b.42.2.0 — automated matches

Domain ID domain_id	d4qd2i3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4qd2j1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.6 — Cadherin-like
Family Family family	b.1.6.1 — Cadherin

Domain ID domain_id	d4qd2j2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.6 — Cadherin-like
Family Family family	b.1.6.1 — Cadherin

CATH v4.4 (16 domains)

Domain ID domain_id	4qd2A02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	1090 —

Domain ID domain_id	4qd2B00
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	4qd2C01
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	4qd2C02
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	4qd2D01
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	4qd2D02
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	4qd2E01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	60 — Cadherins

Domain ID domain_id	4qd2E02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	60 — Cadherins

Domain ID domain_id	4qd2F02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	1090 —

Domain ID domain_id	4qd2G00
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	4qd2H01
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	4qd2H02
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	4qd2I01
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	4qd2I02
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	4qd2J01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	60 — Cadherins

Domain ID domain_id	4qd2J02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	60 — Cadherins

▶

8. Citations (1)

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Unit-cell length a length_a	86.990 Å
Unit-cell length b length_b	95.730 Å
Unit-cell length c length_c	96.140 Å
Unit-cell angle α angle_alpha	116.89 °
Unit-cell angle β angle_beta	96.34 °
Unit-cell angle γ angle_gamma	93.70 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	47.730 Å
R factor r_factor	0.2100
R_work r_work	0.2080
R_free r_free	0.2470

fit	/app/data/saxs_computation/qd/4qd2/4qd2.fit
pddf	/app/data/pr_computation/qd/4qd2/4qd2.pr.out
profile	/app/data/saxs_computation/qd/4qd2/4qd2.dat

Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex

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

Hemagglutinin component HA33

State in the Current Structure

Other States of the Same Protein in the Database

Hemagglutinin component HA17

State in the Current Structure

Other States of the Same Protein in the Database

Hemagglutinin component HA70

State in the Current Structure

Other States of the Same Protein in the Database

Cadherin-1

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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

来源 Source

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

7. Fold Classification (SCOP + CATH) 31 domains

SCOP 2.08 (15 domains)

CATH v4.4 (16 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)