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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P03315 New Search
14PDB entries
22Biological assembly
72chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method 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 Assembly 1 Protein homooligomer Homooligomer；Protein × 240 PDB declaration: 240-MERIC（240） Consistent with protein count
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 Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 3 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric（20） Consistent with protein count
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 Assembly 4 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric（24） Consistent with protein count
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 Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
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 Assembly 2 Other combination Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric（15） Consistent with protein count
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 Assembly 1 Other combination Heteromer；Protein × 17 PDB declaration: heptadecameric（17） Consistent with protein count
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 Assembly 1 Other combination Heteromer；Protein × 16 PDB declaration: 16-meric（16） Consistent with protein count
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 Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: 12-meric（12） Consistent with protein count
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
8X0M Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(5-fold) Deposited 2023-11-04 Assembly 1 Other combination Heteromer；Protein × 11 PDB declaration: 11-meric（11） Consistent with protein count
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 × 2 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 Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric（12） Consistent with protein count
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

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.