← Back to search
1vcq

SEMLIKI FOREST VIRUS CAPSID PROTEIN (CRYSTAL FORM II)

Method: X-RAY DIFFRACTION Dmax: 78.9 Å Quality: GOOD
▼

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

SEMLIKI FOREST VIRUS CAPSID PROTEIN

Semliki forest virus

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 119–267 Chain B； UniProt 119–267 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.10 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 1VCQ 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 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 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
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 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 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 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 1–149； UniProt 119–267 Author chain B； PDBConstruct 1–149； UniProt 119–267

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 1vcq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1vcq
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1vcq
Deposition date deposition_date1996-03-04
Structure title titleSEMLIKI FOREST VIRUS CAPSID PROTEIN (CRYSTAL FORM II)
Keywords keywordsVIRUS COAT PROTEIN, POLYPROTEIN, TRANSMEMBRANE, GLYCOPROTEIN, NUCLEOCAPSID PROTEIN, Viral protein; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION
▼

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

Radius of gyration Rg (Guinier) rg_guinier23.21 Å
Radius of gyration Rg (electron density) rg_electron22.78 Å
Forward intensity I(0) i019172400.00
Molecular weight molecular_weight32457.0 kDa
Excluded volume excluded_volume40354 ų
Envelope volume envelope_volume49363 ų
Hydration-shell volume shell_volume19134 ų
Envelope diameter envelope_diameter79.8 Å
Shell Rg shell_rg28.45 Å
Envelope Rg envelope_rg23.03 Å
Shape Rg shape_rg22.72 Å
Total Rg total_rg23.71 Å
Total atoms total_atoms2284
Residues n_residues298
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
▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax78.9 Å
Rg (real space) rg_real23.35 Å
Rg uncertainty (real space) rg_real_error0.59 Å
I(0) (real space) i0_real1.9170e+07
I(0) uncertainty (real space) i0_real_error2.5970e+05
Rg (reciprocal space) rg_reciprocal23.32 Å
I(0) (reciprocal space) i0_reciprocal19170000.0000
Solution quality estimate total_estimate0.8592
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1 Å
Skewness Skewness skewness0.477
Kurtosis Kurtosis kurtosis-0.366
Angular range angular_range— – 0.3400 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5028000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.775; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.851; Smooth: 0.989
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▼

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1vcqa_
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.3 — Viral proteases
Domain ID domain_idd1vcqb_
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.3 — Viral proteases

CATH v4.4 (4 domains)

Domain ID domain_id1vcqA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1vcqA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1vcqB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1vcqB02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
▶

8. Citations (3)

▶

9. Files and Curves (10)