8x0m

Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(5-fold)

Method: ELECTRON MICROSCOPY D_max: 208.4 Å Quality: GOOD

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

Capsid protein

Semliki Forest virus

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Heteromer Protein × 11 其他Polymer 6 PDB declaration: 11-meric（11） Consistent with protein copy count	Chain A； UniProt 106–267 Chain E； UniProt 106–267 Chain I； UniProt 106–267	Not recorded	Spike glycoprotein E2 × 3 （A0A0E3T652） Spike glycoprotein E1 × 3 （A0A0F6PP03） Very low-density lipoprotein receptor × 2 （P98155） 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.50 Å

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 8X0M	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1DYL 9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY Deposited 2000-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 240 PDB declaration: 240-MERIC	Chain A 119–267（149 aa） Chain B 119–267（149 aa） Chain C 119–267（149 aa） Chain D 119–267（149 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE；PLUNGE VITRIFICATION SAMPLES PREPARED AS THIN LAYERS OF VITREOUS ICE MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626-0300 CRYOTRANSFER HOLDER.	Resolution 9.00 Å
1DYL 9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY Deposited 2000-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 119–267（149 aa） Chain B 119–267（149 aa） Chain C 119–267（149 aa） Chain D 119–267（149 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE；PLUNGE VITRIFICATION SAMPLES PREPARED AS THIN LAYERS OF VITREOUS ICE MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626-0300 CRYOTRANSFER HOLDER.	Resolution 9.00 Å
1DYL 9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY Deposited 2000-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	Chain A 119–267（149 aa） Chain B 119–267（149 aa） Chain C 119–267（149 aa） Chain D 119–267（149 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE；PLUNGE VITRIFICATION SAMPLES PREPARED AS THIN LAYERS OF VITREOUS ICE MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626-0300 CRYOTRANSFER HOLDER.	Resolution 9.00 Å
1DYL 9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY Deposited 2000-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain A 119–267（149 aa） Chain B 119–267（149 aa） Chain C 119–267（149 aa） Chain D 119–267（149 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE；PLUNGE VITRIFICATION SAMPLES PREPARED AS THIN LAYERS OF VITREOUS ICE MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626-0300 CRYOTRANSFER HOLDER.	Resolution 9.00 Å
1DYL 9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY Deposited 2000-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 119–267（149 aa） Chain B 119–267（149 aa） Chain C 119–267（149 aa） Chain D 119–267（149 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE；PLUNGE VITRIFICATION SAMPLES PREPARED AS THIN LAYERS OF VITREOUS ICE MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626-0300 CRYOTRANSFER HOLDER.	Resolution 9.00 Å
1I9W CRYSTAL STRUCTURE OF THE FUSION GLYCOPROTEIN E1 FROM SEMLIKI FOREST VIRUS Deposited 2001-03-21	Different construct Different mutation/modification 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 816–1205（390 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；294 K；PEG 8K, pH 8.0, VAPOR DIFFUSION, temperature 294K	Resolution 3.00 Å R-free 0.344
1RER Crystal structure of the homotrimer of fusion glycoprotein E1 from Semliki Forest Virus. Deposited 2003-11-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 816–1206（391 aa） Fragment：Spike glycoprotein E1 Chain B 816–1206（391 aa） Fragment：Spike glycoprotein E1 Chain C 816–1206（391 aa） Fragment：Spike glycoprotein E1	Not recorded	BR BROMIDE ION × 3 HO HOLMIUM ATOM × 4 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；277 K；PEG 400, NaBr, detergent DDAO, HO3+, VAPOR DIFFUSION, HANGING DROP	Resolution 3.20 Å R-free 0.285
1RER Crystal structure of the homotrimer of fusion glycoprotein E1 from Semliki Forest Virus. Deposited 2003-11-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 816–1206（391 aa） Fragment：Spike glycoprotein E1 Chain B 816–1206（391 aa） Fragment：Spike glycoprotein E1 Chain C 816–1206（391 aa） Fragment：Spike glycoprotein E1	Not recorded	BR BROMIDE ION × 6 HO HOLMIUM ATOM × 8 PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；277 K；PEG 400, NaBr, detergent DDAO, HO3+, VAPOR DIFFUSION, HANGING DROP	Resolution 3.20 Å R-free 0.285
1VCP SEMLIKI FOREST VIRUS CAPSID PROTEIN (CRYSTAL FORM I) Deposited 1996-03-04	Different construct Different mutation/modification 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 119–267（149 aa）	Not recorded	HG MERCURY (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions KHGI4 WAS REQUIRED TO OBTAIN BIG CRYSTALS. EACH OF THREE MONOMERS OF THE SEMLIKI FOREST VIRUS CORE PROTEIN BIND ONE MERCURY ATOM. THE HG ATOM FORMS A S-HG-S BOND WITH CYS 119 AND CYS 134. IN THE NATIVE STRUCTURE THERE IS A DISULFIDE BRIDGE BETWEEN CYS 119 AND CYS 134. THE S-HG DISTANCE WAS RESTRAINED TO 2.45 ANGSTROMS WHILE THE BOND ANGLE OF S-HG-S WAS RESTRAINED TO 180 DEGREES.	Resolution 3.00 Å
1VCP SEMLIKI FOREST VIRUS CAPSID PROTEIN (CRYSTAL FORM I) Deposited 1996-03-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 119–267（149 aa）	Not recorded	HG MERCURY (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions KHGI4 WAS REQUIRED TO OBTAIN BIG CRYSTALS. EACH OF THREE MONOMERS OF THE SEMLIKI FOREST VIRUS CORE PROTEIN BIND ONE MERCURY ATOM. THE HG ATOM FORMS A S-HG-S BOND WITH CYS 119 AND CYS 134. IN THE NATIVE STRUCTURE THERE IS A DISULFIDE BRIDGE BETWEEN CYS 119 AND CYS 134. THE S-HG DISTANCE WAS RESTRAINED TO 2.45 ANGSTROMS WHILE THE BOND ANGLE OF S-HG-S WAS RESTRAINED TO 180 DEGREES.	Resolution 3.00 Å
1VCP SEMLIKI FOREST VIRUS CAPSID PROTEIN (CRYSTAL FORM I) Deposited 1996-03-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 119–267（149 aa）	Not recorded	HG MERCURY (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions KHGI4 WAS REQUIRED TO OBTAIN BIG CRYSTALS. EACH OF THREE MONOMERS OF THE SEMLIKI FOREST VIRUS CORE PROTEIN BIND ONE MERCURY ATOM. THE HG ATOM FORMS A S-HG-S BOND WITH CYS 119 AND CYS 134. IN THE NATIVE STRUCTURE THERE IS A DISULFIDE BRIDGE BETWEEN CYS 119 AND CYS 134. THE S-HG DISTANCE WAS RESTRAINED TO 2.45 ANGSTROMS WHILE THE BOND ANGLE OF S-HG-S WAS RESTRAINED TO 180 DEGREES.	Resolution 3.00 Å
1VCQ SEMLIKI FOREST VIRUS CAPSID PROTEIN (CRYSTAL FORM II) Deposited 1996-03-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 119–267（149 aa） Chain B 119–267（149 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.10 Å
2ALA Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric conformation. Deposited 2005-08-05	Different construct Different mutation/modification 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 816–1206（391 aa） Fragment：Spike glycoprotein E1	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 8.1；293 K；PEG 8K, pH 8.1, EVAPORATION, temperature 293K	Resolution 3.00 Å R-free 0.319
2V33 High resolution crystal structure of domain III of E1 fusion glycoprotein of Semliki Forest Virus Deposited 2007-06-11	Different construct Different mutation/modification 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 1107–1197（91 aa） Fragment：DOMAIN III OF SPIKE GLYCOPROTEIN E1, RESIDUES 1107-1197	Not recorded	NO3 NITRATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；25% PEG 8K, 0.2M NA ACETATE, 0.1M CACO PH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 1.55 Å R-free 0.226
2V33 High resolution crystal structure of domain III of E1 fusion glycoprotein of Semliki Forest Virus Deposited 2007-06-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1107–1197（91 aa） Fragment：DOMAIN III OF SPIKE GLYCOPROTEIN E1, RESIDUES 1107-1197	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；25% PEG 8K, 0.2M NA ACETATE, 0.1M CACO PH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 1.55 Å R-free 0.226
8D87 Fitted crystal structure of the homotrimer of fusion glycoprotein E1 from SFV into subtomogram averaged CHIKV E1 glycoprotein density Deposited 2022-06-08	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 816–1206（391 aa） Fragment：SPIKE GLYCOPROTEIN E1 Chain B 816–1206（391 aa） Fragment：SPIKE GLYCOPROTEIN E1 Chain C 816–1206（391 aa） Fragment：SPIKE GLYCOPROTEIN E1	Not recorded	BR BROMIDE ION × 3 HO HOLMIUM ATOM × 4 PO4 PHOSPHATE ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 5.1；Hepes Buffer Saline cryo-EM vitrification conditions Cryogen ETHANE；blot for 7-8 seconds X-ray crystallization conditions pH 4；PEG 400, NABR, DETERGENT DDAO, HO3+, VAPOR DIFFUSION, HANGING DROP, PH 4, TEMPERATURE 277.0K	Resolution 27.20 Å R-free 0.285
8IHP Structure of Semliki Forest virus VLP in complex with the receptor VLDLR-LA3 Deposited 2023-02-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric	Chain A 334–755（422 aa） Chain B 816–1253（438 aa） Chain C 106–267（162 aa） Chain D 334–755（422 aa） Chain E 816–1253（438 aa） Chain F 106–267（162 aa） Chain G 334–755（422 aa） Chain H 816–1253（438 aa） Chain I 106–267（162 aa） Chain J 334–755（422 aa） Chain K 816–1253（438 aa） Chain L 106–267（162 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 CA CALCIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
8UA8 Structure of Semliki Forest virus VLP in complex with VLDLR LA2 Deposited 2023-09-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 17 PDB declaration: heptadecameric	Chain C 273–326（54 aa） Chain D 115–267（153 aa） Chain G 273–326（54 aa） Chain H 115–267（153 aa） Chain K 273–326（54 aa） Chain L 115–267（153 aa） Chain O 273–326（54 aa） Chain P 115–267（153 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
8X0K Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(2-fold) Deposited 2023-11-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion	Assembly 1 Other combination Heteromer；Protein × 16 PDB declaration: 16-meric	Chain A 106–267（162 aa） Chain E 106–267（162 aa） Chain I 106–267（162 aa） Chain M 106–267（162 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CA CALCIUM ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8X0L Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(3-fold) Deposited 2023-11-04	Different oligomeric state Different ligand/ion	Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: 12-meric	Chain A 106–267（162 aa） Chain E 106–267（162 aa） Chain I 106–267（162 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9KQR Cryo-EM Structure of Mature Semliki Forest Virus Deposited 2024-11-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric	Chain a 816–1253（438 aa） Chain d 816–1253（438 aa） Chain g 816–1253（438 aa） Chain j 816–1253（438 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.73 Å

13 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	POLS_SFV
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–162； UniProt 106–267 Author chain E； PDBConstruct 1–162； UniProt 106–267 Author chain I； PDBConstruct 1–162； UniProt 106–267

Spike glycoprotein E2

Semliki Forest virus

UniProt A0A0E3T652

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Heteromer Protein × 11 其他Polymer 6 PDB declaration: 11-meric（11） Consistent with protein copy count	Chain B； UniProt 334–751 Chain F； UniProt 334–751 Chain J； UniProt 334–751	Not recorded	Capsid protein × 3 （P03315） Spike glycoprotein E1 × 3 （A0A0F6PP03） Very low-density lipoprotein receptor × 2 （P98155） 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.50 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8X0M	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8UA8 Structure of Semliki Forest virus VLP in complex with VLDLR LA2 Deposited 2023-09-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 17 PDB declaration: heptadecameric	Chain B 339–755（417 aa） Chain F 339–755（417 aa） Chain J 339–755（417 aa） Chain N 339–755（417 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
8X0K Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(2-fold) Deposited 2023-11-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion	Assembly 1 Other combination Heteromer；Protein × 16 PDB declaration: 16-meric	Chain B 334–751（418 aa） Chain F 334–751（418 aa） Chain J 334–751（418 aa） Chain N 334–751（418 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CA CALCIUM ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8X0L Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(3-fold) Deposited 2023-11-04	Different oligomeric state Different ligand/ion	Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: 12-meric	Chain B 334–751（418 aa） Chain F 334–751（418 aa） Chain J 334–751（418 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8YVY Semliki Forest virus virion Deposited 2024-03-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 816–1253（438 aa） Chain B 338–755（418 aa） Chain C 275–326（52 aa） Chain D 107–267（161 aa） Chain F 816–1253（438 aa） Chain G 816–1253（438 aa） Chain H 816–1253（438 aa） Chain I 338–755（418 aa） Chain J 338–755（418 aa） Chain K 338–755（418 aa） Chain L 275–326（52 aa） Chain M 275–326（52 aa） Chain N 275–326（52 aa） Chain O 107–267（161 aa） Chain P 107–267（161 aa） Chain Q 107–267（161 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.02 Å
8YVZ Semliki Forest virus viron Deposited 2024-03-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 20 PDB declaration: eicosameric	Chain A 816–1253（438 aa） Chain B 338–755（418 aa） Chain C 275–326（52 aa） Chain D 107–267（161 aa） Chain F 816–1253（438 aa） Chain G 816–1253（438 aa） Chain H 816–1253（438 aa） Chain I 338–755（418 aa） Chain J 338–755（418 aa） Chain K 338–755（418 aa） Chain L 275–326（52 aa） Chain M 275–326（52 aa） Chain N 275–326（52 aa） Chain O 107–267（161 aa） Chain P 107–267（161 aa） Chain Q 107–267（161 aa）	Not recorded	CA CALCIUM ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.45 Å
8YW0 Semliki Forest virus viron Deposited 2024-03-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 19 PDB declaration: nonadecameric	Chain A 816–1253（438 aa） Chain B 338–755（418 aa） Chain C 275–326（52 aa） Chain D 107–267（161 aa） Chain F 816–1253（438 aa） Chain G 816–1253（438 aa） Chain H 816–1253（438 aa） Chain I 338–755（418 aa） Chain J 338–755（418 aa） Chain K 338–755（418 aa） Chain L 275–326（52 aa） Chain M 275–326（52 aa） Chain N 275–326（52 aa） Chain O 107–267（161 aa） Chain P 107–267（161 aa） Chain Q 107–267（161 aa）	Not recorded	CA CALCIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.55 Å
8YW1 Semliki Forest virus viron in complex with VLDLR Deposited 2024-03-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 33 PDB declaration: 33-meric	Chain A 816–1253（438 aa） Chain B 338–755（418 aa） Chain D 107–267（161 aa） Chain E 816–1253（438 aa） Chain F 816–1253（438 aa） Chain G 816–1253（438 aa） Chain H 816–1253（438 aa） Chain I 338–755（418 aa） Chain J 338–755（418 aa） Chain K 338–755（418 aa） Chain L 275–326（52 aa） Chain M 275–326（52 aa） Chain N 275–326（52 aa） Chain O 107–267（161 aa） Chain P 107–267（161 aa） Chain Q 107–267（161 aa） Chain R 338–755（418 aa） Chain S 275–326（52 aa） Chain T 107–267（161 aa） Chain U 816–1253（438 aa） Chain V 816–1253（438 aa） Chain W 816–1253（438 aa） Chain X 338–755（418 aa） Chain Y 338–755（418 aa） Chain Z 338–755（418 aa） Chain a 275–326（52 aa） Chain b 275–326（52 aa） Chain c 275–326（52 aa） Chain d 107–267（161 aa） Chain e 107–267（161 aa） Chain f 107–267（161 aa） Chain g 275–326（52 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.44 Å
8YW2 Semliki Forest virus viron in complex with VLDLR Deposited 2024-03-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 65 PDB declaration: 65-meric	Chain 0 275–326（52 aa） Chain 1 107–267（161 aa） Chain 2 275–326（52 aa） Chain 3 107–267（161 aa） Chain 4 816–1253（438 aa） Chain 5 816–1253（438 aa） Chain 6 816–1253（438 aa） Chain 7 338–755（418 aa） Chain 8 338–755（418 aa） Chain 9 338–755（418 aa） Chain AA 275–326（52 aa） Chain AB 275–326（52 aa） Chain AC 107–267（161 aa） Chain AD 107–267（161 aa） Chain AE 107–267（161 aa） Chain B 338–755（418 aa） Chain D 107–267（161 aa） Chain E 816–1253（438 aa） Chain F 816–1253（438 aa） Chain G 816–1253（438 aa） Chain H 816–1253（438 aa） Chain I 338–755（418 aa） Chain J 338–755（418 aa） Chain K 338–755（418 aa） Chain L 275–326（52 aa） Chain M 275–326（52 aa） Chain N 275–326（52 aa） Chain O 107–267（161 aa） Chain P 107–267（161 aa） Chain Q 107–267（161 aa） Chain R 338–755（418 aa） Chain S 275–326（52 aa） Chain T 107–267（161 aa） Chain U 816–1253（438 aa） Chain V 816–1253（438 aa） Chain W 816–1253（438 aa） Chain X 338–755（418 aa） Chain Y 338–755（418 aa） Chain Z 338–755（418 aa） Chain a 275–326（52 aa） Chain b 275–326（52 aa） Chain c 275–326（52 aa） Chain d 107–267（161 aa） Chain e 107–267（161 aa） Chain f 107–267（161 aa） Chain g 275–326（52 aa） Chain h 816–1253（438 aa） Chain i 816–1253（438 aa） Chain j 338–755（418 aa） Chain l 275–326（52 aa） Chain m 816–1253（438 aa） Chain n 107–267（161 aa） Chain o 816–1253（438 aa） Chain p 816–1253（438 aa） Chain q 816–1253（438 aa） Chain r 338–755（418 aa） Chain s 338–755（418 aa） Chain t 338–755（418 aa） Chain u 275–326（52 aa） Chain v 275–326（52 aa） Chain w 275–326（52 aa） Chain x 107–267（161 aa） Chain y 107–267（161 aa） Chain z 338–755（418 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A0E3T652_SFV
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–418； UniProt 334–751 Author chain F； PDBConstruct 1–418； UniProt 334–751 Author chain J； PDBConstruct 1–418； UniProt 334–751

Spike glycoprotein E1

Semliki Forest virus

UniProt A0A0F6PP03

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Heteromer Protein × 11 其他Polymer 6 PDB declaration: 11-meric（11） Consistent with protein copy count	Chain C； UniProt 816–1253 Chain G； UniProt 816–1253 Chain K； UniProt 816–1253	Not recorded	Capsid protein × 3 （P03315） Spike glycoprotein E2 × 3 （A0A0E3T652） Very low-density lipoprotein receptor × 2 （P98155） 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.50 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8X0M	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8UA8 Structure of Semliki Forest virus VLP in complex with VLDLR LA2 Deposited 2023-09-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 17 PDB declaration: heptadecameric	Chain A 816–1253（438 aa） Chain E 816–1253（438 aa） Chain I 816–1253（438 aa） Chain M 816–1253（438 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
8X0K Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(2-fold) Deposited 2023-11-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion	Assembly 1 Other combination Heteromer；Protein × 16 PDB declaration: 16-meric	Chain C 816–1253（438 aa） Chain G 816–1253（438 aa） Chain K 816–1253（438 aa） Chain O 816–1253（438 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CA CALCIUM ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8X0L Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(3-fold) Deposited 2023-11-04	Different oligomeric state Different ligand/ion	Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: 12-meric	Chain C 816–1253（438 aa） Chain G 816–1253（438 aa） Chain K 816–1253（438 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9RBQ Semliki Forest virus trimer 1 in complex with ApoER2 LA5 Deposited 2025-05-27	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 13 PDB declaration: 13-meric	Chain G 816–1253（438 aa） Chain H 816–1253（438 aa） Chain I 816–1253（438 aa）	Not recorded	CA CALCIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
9RBR Semliki Forest virus trimer 2 in complex with ApoER2 LA5 Deposited 2025-05-27	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: dodecameric	Chain G 816–1253（438 aa） Chain H 816–1253（438 aa） Chain I 816–1253（438 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A0F6PP03_SFV
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–438； UniProt 816–1253 Author chain G； PDBConstruct 1–438； UniProt 816–1253 Author chain K； PDBConstruct 1–438； UniProt 816–1253

Very low-density lipoprotein receptor

Semliki Forest virus

UniProt P98155

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Heteromer Protein × 11 其他Polymer 6 PDB declaration: 11-meric（11） Consistent with protein copy count	Chain D； UniProt 113–149 Chain H； UniProt 113–149	Not recorded	Capsid protein × 3 （P03315） Spike glycoprotein E2 × 3 （A0A0E3T652） Spike glycoprotein E1 × 3 （A0A0F6PP03） 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.50 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8X0M	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1V9U Human Rhinovirus 2 bound to a fragment of its cellular receptor protein Deposited 2004-02-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 300 PDB declaration: complete icosahedral assembly	Chain 5 111–151（41 aa）	Not recorded	DAO LAURIC ACID × 60 CA CALCIUM ION × 60	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；Ammonim sulfate, sodium/potassium phosphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.60 Å R-free 0.295
1V9U Human Rhinovirus 2 bound to a fragment of its cellular receptor protein Deposited 2004-02-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain 5 111–151（41 aa）	Not recorded	DAO LAURIC ACID × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；Ammonim sulfate, sodium/potassium phosphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.60 Å R-free 0.295
1V9U Human Rhinovirus 2 bound to a fragment of its cellular receptor protein Deposited 2004-02-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 25 PDB declaration: 25-meric	Chain 5 111–151（41 aa）	Not recorded	DAO LAURIC ACID × 5 CA CALCIUM ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；Ammonim sulfate, sodium/potassium phosphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.60 Å R-free 0.295
1V9U Human Rhinovirus 2 bound to a fragment of its cellular receptor protein Deposited 2004-02-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain 5 111–151（41 aa）	Not recorded	DAO LAURIC ACID × 6 CA CALCIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；Ammonim sulfate, sodium/potassium phosphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.60 Å R-free 0.295
1V9U Human Rhinovirus 2 bound to a fragment of its cellular receptor protein Deposited 2004-02-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain 5 111–151（41 aa）	Not recorded	DAO LAURIC ACID × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；Ammonim sulfate, sodium/potassium phosphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.60 Å R-free 0.295
1V9U Human Rhinovirus 2 bound to a fragment of its cellular receptor protein Deposited 2004-02-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 150 PDB declaration: 150-meric	Chain 5 111–151（41 aa）	Not recorded	DAO LAURIC ACID × 30 CA CALCIUM ION × 30	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；Ammonim sulfate, sodium/potassium phosphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.60 Å R-free 0.295
3DPR Human rhinovirus 2 bound to a concatamer of the VLDL receptor module V3 Deposited 2008-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 300 PDB declaration: 300-MERIC	Chain E 113–151（39 aa）	Not recorded	DAO LAURIC ACID × 60 CA CALCIUM ION × 60	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；Ammonium sulphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.50 Å R-free 0.441
3DPR Human rhinovirus 2 bound to a concatamer of the VLDL receptor module V3 Deposited 2008-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 113–151（39 aa）	Not recorded	DAO LAURIC ACID × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；Ammonium sulphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.50 Å R-free 0.441
3DPR Human rhinovirus 2 bound to a concatamer of the VLDL receptor module V3 Deposited 2008-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 25 PDB declaration: 25-meric	Chain E 113–151（39 aa）	Not recorded	DAO LAURIC ACID × 5 CA CALCIUM ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；Ammonium sulphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.50 Å R-free 0.441
3DPR Human rhinovirus 2 bound to a concatamer of the VLDL receptor module V3 Deposited 2008-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain E 113–151（39 aa）	Not recorded	DAO LAURIC ACID × 6 CA CALCIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；Ammonium sulphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.50 Å R-free 0.441
3DPR Human rhinovirus 2 bound to a concatamer of the VLDL receptor module V3 Deposited 2008-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 113–151（39 aa）	Not recorded	DAO LAURIC ACID × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；Ammonium sulphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.50 Å R-free 0.441
3DPR Human rhinovirus 2 bound to a concatamer of the VLDL receptor module V3 Deposited 2008-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 300 PDB declaration: 300-meric	Chain E 113–151（39 aa）	Not recorded	DAO LAURIC ACID × 60 CA CALCIUM ION × 60	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；Ammonium sulphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.50 Å R-free 0.441
6BYV Solution NMR structure of cysteine-rich calcium bound domains of very low density lipoprotein receptor Deposited 2017-12-21	Different construct Different mutation/modification 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 70–190（121 aa）	Not recorded	CA CALCIUM ION × 3	SOLUTION NMR NMR measurement conditions pH 6.2；306.5 K；Ionic strength (raw mmCIF value) 100；Pressure 760 NMR measurement conditions pH 6.2；306.5 K；Ionic strength (raw mmCIF value) 100；Pressure 760 NMR sample composition 350 uM [U-99% 15N] VLDLR, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition 250 uM [U-99% 13C; U-99% 15N] VLDLR, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition 250 uM [U-99% 13C; U-99% 15N] VLDLR, 100% D2O \| 100% D2O	Resolution not provided
8IHP Structure of Semliki Forest virus VLP in complex with the receptor VLDLR-LA3 Deposited 2023-02-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric	Chain M 111–149（39 aa） Chain N 111–149（39 aa） Chain O 111–149（39 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 CA CALCIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
8UA4 Structure of eastern equine encephalitis virus VLP in complex with VLDLR LA1 Deposited 2023-09-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 17 PDB declaration: heptadecameric	Chain R 33–68（36 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 CA CALCIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.58 Å
8UA8 Structure of Semliki Forest virus VLP in complex with VLDLR LA2 Deposited 2023-09-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 17 PDB declaration: heptadecameric	Chain R 72–108（37 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
8UFB Eastern equine encephalitis virus (PE-6) VLP in complex with full-length VLDLR (asymmetric unit) Deposited 2023-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain R 28–769（742 aa） Chain S 28–769（742 aa） Chain T 28–769（742 aa） Chain U 28–769（742 aa） Chain V 28–769（742 aa） Chain W 28–769（742 aa） Chain X 28–769（742 aa） Chain Y 28–769（742 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.89 Å
8UFC Eastern equine encephalitis virus (PE-6) VLP in complex with VLDLR LA(1-2) (asymmetric unit) Deposited 2023-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain V 31–108（78 aa） Fragment：UNP residues 31-108 Chain W 31–108（78 aa） Fragment：UNP residues 31-108 Chain X 31–108（78 aa） Fragment：UNP residues 31-108 Chain Y 31–108（78 aa） Fragment：UNP residues 31-108	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.09 Å
8X0K Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(2-fold) Deposited 2023-11-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion	Assembly 1 Other combination Heteromer；Protein × 16 PDB declaration: 16-meric	Chain D 113–149（37 aa） Chain H 113–149（37 aa） Chain L 113–149（37 aa） Chain P 113–149（37 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CA CALCIUM ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8X0L Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(3-fold) Deposited 2023-11-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion	Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: 12-meric	Chain D 113–149（37 aa） Chain H 113–149（37 aa） Chain L 113–149（37 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8XI4 Structure of Eastern Equine Encephalitis VLP in complex with the receptor VLDLR LA1-2 Deposited 2023-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric	Chain M 31–113（83 aa） Chain N 31–113（83 aa） Chain O 31–113（83 aa） Chain P 31–113（83 aa）	Not recorded	CA CALCIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
8XI5 Structure of Eastern Equine Encephalitis VLP in complex with the receptor VLDLR LA3-5 Deposited 2023-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric	Chain M 191–231（41 aa） Chain N 191–231（41 aa） Chain O 191–231（41 aa） Chain P 191–231（41 aa） Chain Q 111–151（41 aa） Chain R 111–151（41 aa） Chain S 111–151（41 aa） Chain T 111–151（41 aa）	Not recorded	CA CALCIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
8YS2 Overall structure of Eastern Equine Encephalitis virus VLP in complex with the receptor VLDLR LA1-2 Deposited 2024-03-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 960 PDB declaration: 960-meric	Chain M 31–110（80 aa） Chain N 31–110（80 aa） Chain O 31–110（80 aa） Chain P 31–110（80 aa）	Not recorded	CA CALCIUM ION × 480	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.20 Å
8YS4 Overall structure of Eastern Equine Encephalitis virus VLP in complex with the receptor VLDLR LA3-5 Deposited 2024-03-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 1200 PDB declaration: 1200-meric	Chain M 191–231（41 aa） Chain N 191–231（41 aa） Chain O 191–231（41 aa） Chain P 191–231（41 aa） Chain Q 111–151（41 aa） Chain R 111–151（41 aa） Chain S 111–151（41 aa） Chain T 111–151（41 aa）	Not recorded	CA CALCIUM ION × 480	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.80 Å
8YVZ Semliki Forest virus viron Deposited 2024-03-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 20 PDB declaration: eicosameric	Chain E 110–151（42 aa） Chain R 110–151（42 aa） Chain S 110–151（42 aa） Chain T 110–151（42 aa）	Not recorded	CA CALCIUM ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.45 Å
8YW0 Semliki Forest virus viron Deposited 2024-03-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 19 PDB declaration: nonadecameric	Chain E 191–230（40 aa） Chain R 191–230（40 aa） Chain T 191–230（40 aa）	Not recorded	CA CALCIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.55 Å
8YW1 Semliki Forest virus viron in complex with VLDLR Deposited 2024-03-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 33 PDB declaration: 33-meric	Chain C 111–231（121 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.44 Å
8YW2 Semliki Forest virus viron in complex with VLDLR Deposited 2024-03-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 65 PDB declaration: 65-meric	Chain A 70–231（162 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
9DQZ Structure of western equine encephalitis virus McMillan VLP in complex with human VLDLR Deposited 2024-09-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric	Chain M 33–110（78 aa） Chain N 33–110（78 aa） Chain O 33–110（78 aa） Chain P 33–110（78 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 CA CALCIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
9E9Y WEEV McMillan VLP in complex with VLDLR LA(1-2) Deposited 2024-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric	Chain V 31–108（78 aa） Fragment：UNP residues 31-108 Chain X 31–108（78 aa） Fragment：UNP residues 31-108 Chain Y 31–108（78 aa） Fragment：UNP residues 31-108 Chain Z 31–108（78 aa） Fragment：UNP residues 31-108	Not recorded	CA CALCIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.96 Å
9E9Z SINV-WEEV Fleming in complex with VLDLR LA(1-2) Deposited 2024-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric	Chain V 31–108（78 aa） Fragment：UNP residues 31-108 Chain W 31–108（78 aa） Fragment：UNP residues 31-108 Chain X 31–108（78 aa） Fragment：UNP residues 31-108 Chain Y 31–108（78 aa） Fragment：UNP residues 31-108	Not recorded	CA CALCIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.95 Å
9EAU RRV DKTA VLP in complex with VLDLR-LBD-Fc Deposited 2024-11-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: 14-meric	Chain Y 111–149（39 aa） Chain Z 111–149（39 aa）	Not recorded	CA CALCIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.06 Å
9L99 Structure of Western equine encephalitis virus McMillan strain in complex with VLDLR LA1-2 Deposited 2024-12-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain N 31–110（80 aa）	Not recorded	CA CALCIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
9L9A Structure of Western equine encephalitis virus McMillan strain in complex with VLDLR LA2-3 Deposited 2024-12-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain M 70–151（82 aa）	Not recorded	CA CALCIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
9WSL CryoEM structure of Western equine encephalitis virus California VLP in complex with VLDLR-LBD Deposited 2025-09-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain R 32–110（79 aa） Chain S 32–110（79 aa） Chain T 32–110（79 aa）	Not recorded	CA CALCIUM ION × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.27 Å

25 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	VLDLR_HUMAN
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain D； PDBConstruct 1–37； UniProt 113–149 Author chain H； PDBConstruct 1–37； UniProt 113–149

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	8x0m
Deposition date deposition_date	2023-11-04
Structure title title	Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(5-fold)
Keywords keywords	VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	63.16 Å
Radius of gyration Rg (electron density) rg_electron	62.60 Å
Forward intensity I(0) i0	1767770000.00
Molecular weight molecular_weight	346050.0 kDa
Excluded volume excluded_volume	429950 Å³
Envelope volume envelope_volume	773580 Å³
Hydration-shell volume shell_volume	104190 Å³
Envelope diameter envelope_diameter	195.9 Å
Shell Rg shell_rg	64.66 Å
Envelope Rg envelope_rg	59.95 Å
Shape Rg shape_rg	62.51 Å
Total Rg total_rg	62.97 Å
Total atoms total_atoms	24274
Residues n_residues	3128
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	208.4 Å
Rg (real space) rg_real	63.04 Å
Rg uncertainty (real space) rg_real_error	1.86 Å
I(0) (real space) i0_real	1.7680e+09
I(0) uncertainty (real space) i0_real_error	3.8930e+07
Rg (reciprocal space) rg_reciprocal	63.21 Å
I(0) (reciprocal space) i0_reciprocal	1768000000.0000
Solution quality estimate total_estimate	0.8773
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	66.7 Å
Skewness Skewness skewness	0.162
Kurtosis Kurtosis kurtosis	-0.662
Angular range angular_range	— – 0.1250 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	89530000.0000
Real-space data points n_real_points	26
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.634

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	Capsid protein
Molecular weight formula_weight	17848.3 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,E,I
Atom count atom_count	24274

GKRERMCMKIENDCIFEVKHEGKVTGYACLVGDKVMKPAHVKGVIDNADLAKLAFKKSSKYDLECAQIPVHMRSDASKYTHEKPEGHYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGSRTALSVVTWNKDMVTRVTPEGSEEW

来源 Source

来源生物 organism	Semliki Forest virus
NCBI Class编号 ncbi_taxonomy_id	11033
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	Spike glycoprotein E2
Molecular weight formula_weight	46432.8 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,F,J

SVSQHFNVYKATRPYIAYCADCGAGHSCHSPVAIEAVRSEATDGMLKIQFSAQIGIDKSDNHDYTKIRYADGHAIENAVRSSLKVATSGDCFVHGTMGHFILAKCPPGEFLQVSIQDTRNAVRACRIQYHHDPQPVGREKFTIRPHYGKEIPCTTYQQTTAKTVEEIDMHMPPDTPDRTLLSQQSGNVKITVGGKKVKYNCTCGTGNVGTTNSDMTINTCLIEQCHVSVTDHKKWQFNSPFVPRADEPARKGKVHIPFPLDNITCRVPMAREPTVIHGKREVTLHLHPDHPTLFSYRTLGEDPQYHEEWVTAAVERTIPVPVDGMEYHWGNNDPVRLWSQLTTEGKPHGWPHQIVQYYYGLYPAATVSAVVGMSLLALISIFASCYMLVAARSKCLTPYALTPGAAVPWTLGILCCAP

来源 Source

来源生物 organism	Semliki Forest virus
NCBI Class编号 ncbi_taxonomy_id	11033
宿主生物 host_organism	Homo sapiens

Entity 3 Entity 3 polymer

Description description	Spike glycoprotein E1
Molecular weight formula_weight	47489.8 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,G,K

YEHSTVMPNVVGFPYKAHIERPGYSPLTLQMQVVETSLEPTLNLEYITCEYKTVVPSPYVKCCGASECSTKEKPDYQCKVYTGVYPFMWGGAYCFCDSENTQLSEAYVDRSDVCRHDHASAYKAHTASLKAKVRVMYGNVNQTVDVYVNGDHAVTIGGTQFIFGPLSSAWTPFDNKIVVYKDEVFNQDFPPYGSGQPGRFGDIQSRTVESNDLYANTALKLARPSPGMVHVPYTQTPSGFKYWLKEKGTALNTKAPFGCQIKTNPVRAMNCAVGNIPVSMNLPDSAFTRIVEAPTIIDLTCTVATCTHSSDFGGVLTLTYKTDKNGDCSVHSHSNVATLQEATAKVKTAGKVTLHFSTASASPSFVVSLCSARATCSASCEPPKDHIVPYAASHSNVVFPDMSGTALSWVQKISGGLGAFAIGAILVLVVVTCIGLRR

来源 Source

来源生物 organism	Semliki Forest virus
NCBI Class编号 ncbi_taxonomy_id	11033
宿主生物 host_organism	Homo sapiens

Entity 4 Entity 4 polymer

Description description	Very low-density lipoprotein receptor
Molecular weight formula_weight	4103.4 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,H

CRIHEISCGAHSTQCIPVSWRCDGENDCDSGEDEENC

来源 Source

来源生物 organism	Semliki Forest virus
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 5 Entity 5 branched

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	424.4 kDa
Source method src_method	man
Copy count entity_count	6

Entity 6 Entity 6 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 7 Entity 7 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	2

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8. Citations (1)

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

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

Resolution resolution	3.50 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	751970

fit	/app/data/saxs_computation/x0/8x0m/8x0m.fit
pddf	/app/data/pr_computation/x0/8x0m/8x0m.pr.out
profile	/app/data/saxs_computation/x0/8x0m/8x0m.dat

Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(5-fold)

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

Capsid protein

State in the Current Structure

Other States of the Same Protein in the Database

Spike glycoprotein E2

State in the Current Structure

Other States of the Same Protein in the Database

Spike glycoprotein E1

State in the Current Structure

Other States of the Same Protein in the Database

Very low-density lipoprotein receptor

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (7)

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 branched

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)