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2ala

Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric conformation.

Method: X-RAY DIFFRACTION Dmax: 129.3 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Structural polyprotein (P130)

OrganismNot specified

UniProt P03315

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 816–1206 Fragment：Spike glycoprotein E1 No other associated polymer 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

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 2ALA 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 experimental method 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 experimental method 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 experimental method 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 experimental method 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 experimental method 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 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 mutation/modification 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 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 mutation/modification Different oligomeric state Different ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 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
2V33 High resolution crystal structure of domain III of E1 fusion glycoprotein of Semliki Forest Virus Deposited 2007-06-11 Different construct Different ligand/ion 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 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 mutation/modification 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 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 experimental method Different experimental conditions 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 method 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 Different experimental method Different experimental conditions Different structure-quality metrics 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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 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
8X0M Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(5-fold) Deposited 2023-11-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 11 PDB declaration: 11-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 × 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 Different construct Different mutation/modification Different oligomeric state Different experimental method 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 1–391； UniProt 816–1206

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 2ala

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ala
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ala
Deposition date deposition_date2005-08-05
Structure title titleCrystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric conformation.
Keywords keywordsEnvelope glycoprotein, Membrane Fusion, Viral protein; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier35.43 Å
Radius of gyration Rg (electron density) rg_electron36.37 Å
Forward intensity I(0) i029197700.00
Molecular weight molecular_weight41833.0 kDa
Excluded volume excluded_volume52059 ų
Envelope volume envelope_volume70399 ų
Hydration-shell volume shell_volume20009 ų
Envelope diameter envelope_diameter133.5 Å
Shell Rg shell_rg33.89 Å
Envelope Rg envelope_rg36.33 Å
Shape Rg shape_rg36.30 Å
Total Rg total_rg36.40 Å
Total atoms total_atoms2935
Residues n_residues384
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax129.3 Å
Rg (real space) rg_real36.28 Å
Rg uncertainty (real space) rg_real_error1.70 Å
I(0) (real space) i0_real2.9200e+07
I(0) uncertainty (real space) i0_real_error5.1490e+05
Rg (reciprocal space) rg_reciprocal35.75 Å
I(0) (reciprocal space) i0_reciprocal29180000.0000
Solution quality estimate total_estimate0.6388
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary20.1 Å
Skewness Skewness skewness0.676
Kurtosis Kurtosis kurtosis-0.353
Angular range angular_range— – 0.2250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1362000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.245; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.062; Smooth: 0.504
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2alaa1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.0 — automated matches
Domain ID domain_idd2alaa2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.10 — Viral glycoprotein, central and dimerisation domains
Superfamily Superfamily superfamilyf.10.1 — Viral glycoprotein, central and dimerisation domains
Family Family familyf.10.1.1 — Viral glycoprotein, central and dimerisation domains

CATH v4.4 (2 domains)

Domain ID domain_id2alaA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology98 — Tick-borne Encephalitis virus Glycoprotein; domain 1
Homologous superfamily homologous superfamily10 — Tick-borne Encephalitis virus Glycoprotein, domain 1
Domain ID domain_id2alaA03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily350 —
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8. Citations (3)

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9. Files and Curves (10)