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1wpo

HYDROLYTIC ENZYME HUMAN CYTOMEGALOVIRUS PROTEASE

Method: X-RAY DIFFRACTION Dmax: 83.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

HUMAN CYTOMEGALOVIRUS PROTEASE

Human herpesvirus 5

UniProt P16753

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 1–256 Chain B； UniProt 1–256 Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å R-free 0.288

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 1WPO Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CMV HUMAN CYTOMEGALOVIRUS PROTEASE Deposited 1996-08-26 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–256（256 aa）
Chain B 1–256（256 aa）
Mutation：V141A, A144P Mutation：V141A, A144P No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；28-30% MONOMETHYL POLYETHYLENE GLYCOL 550 0.05-0.2 M NACL 10% GLYCEROL 50 MM HEPES AT PH 7.5
Resolution 2.27 Å R-free 0.310
1ID4 CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157Q) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE Deposited 2001-04-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–256（256 aa） Fragment：RESIDUES 1-256
Chain B 1–256（256 aa） Fragment：RESIDUES 1-256
Mutation：A143Q, H157Q Mutation：A143Q, H157Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；294 K；19% PEG 3350, 0.1M MES 6.0, 15% Glycerol, 5% t-BuOH, 0.4M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 294K
Resolution 2.20 Å R-free 0.262
1IEC CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157A) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE Deposited 2001-04-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–256（256 aa） Fragment：RESIDUES 1-256
Chain B 1–256（256 aa） Fragment：RESIDUES 1-256
Mutation：A143Q, H157A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：A143Q, H157A Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；294 K；20% PEG3350, 0.1M MES 6.0, 15% GLYCEROL, 5% t-BuOH, 0.3M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 294K
Resolution 2.20 Å R-free 0.269
1IED CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157E) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE Deposited 2001-04-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–256（256 aa） Fragment：RESIDUES 1-256
Chain B 1–256（256 aa） Fragment：RESIDUES 1-256
Mutation：A143Q, H157E Mutation：A143Q, H157E No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；294 K；21% PEG3350, 0.1M MES 6.0, 15% GLYCEROL, 5% t-BuOH, 0.4M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 294K
Resolution 2.00 Å R-free 0.269
1IEF CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT S134A OF THE HUMAN CYTOMEGALOVIRUS PROTEASE Deposited 2001-04-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–256（256 aa） Fragment：RESIDUES 1-256
Chain B 1–256（256 aa） Fragment：RESIDUES 1-256
Mutation：A143Q, S134A Mutation：A143Q, S134A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；294 K；20% PEG3350, 0.1M MES 6.0, 15% GLYCEROL, 5% t-BuOH, 0.3M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 294K
Resolution 2.30 Å R-free 0.270
1IEG CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT S134A/H157A OF THE HUMAN CYTOMEGALOVIRUS PROTEASE Deposited 2001-04-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–256（256 aa） Fragment：RESIDUES 1-256
Chain B 1–256（256 aa） Fragment：RESIDUES 1-256
Mutation：A143Q, S134A, H157A Mutation：A143Q, S134A, H157A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；294 K；19% PEG3350, 0.1M MES 6.0, 15% GLYCEROL, 5% t-BuOH, 0.3M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 294K
Resolution 2.00 Å R-free 0.259
1JQ6 HUMAN CYTOMEGALOVIRUS PROTEASE DIMER-INTERFACE MUTANT, S225Y Deposited 2001-08-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–256（256 aa）
Mutation：A143Q, S225Y Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；294 K；PEG 8000, sodium cacodylate, magnesium acetate, glycerol, spermine tetrahydrochloride, DTT, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 294K
Resolution 2.30 Å R-free 0.286
1JQ7 HCMV protease dimer-interface mutant, S225Y complexed to Inhibitor BILC 408 Deposited 2001-08-03 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–256（256 aa）
Chain B 1–256（256 aa）
Mutation：A143Q, S225Y Mutation：A143Q, S225Y 0FP N-(6-aminohexanoyl)-3-methyl-L-valyl-3-methyl-L-valyl-N~1~-[(2S,3S)-3-hydroxy-4-oxo-4-{[(1R)-1-phenylpropyl]amino}butan-2-yl]-N~4~,N~4~-dimethyl-L-aspartamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；PEG 4000, HEPES, sodium chloride, glycerol, spermine tetrahydrochloride, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
Resolution 3.00 Å R-free 0.339
1LAY CRYSTAL STRUCTURE OF CYTOMEGALOVIRUS PROTEASE Deposited 1996-07-16 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–256（256 aa）
Mutation：A143V No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å
1NJT COMPLEX STRUCTURE OF HCMV PROTEASE AND A PEPTIDOMIMETIC INHIBITOR Deposited 2003-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–256（256 aa） Fragment：Assemblin
Chain B 1–256（256 aa） Fragment：Assemblin
Mutation：A143Q Mutation：A143Q CL CHLORIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；PEG 4000, HEPES, EDTA, Sodium Chloride, Sodium Sulfate, DTT, Spermine_HCl, Glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.50 Å R-free 0.271
1NJT COMPLEX STRUCTURE OF HCMV PROTEASE AND A PEPTIDOMIMETIC INHIBITOR Deposited 2003-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–256（256 aa） Fragment：Assemblin
Chain D 1–256（256 aa） Fragment：Assemblin
Mutation：A143Q Mutation：A143Q CL CHLORIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；PEG 4000, HEPES, EDTA, Sodium Chloride, Sodium Sulfate, DTT, Spermine_HCl, Glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.50 Å R-free 0.271
1NJU Complex structure of HCMV Protease and a peptidomimetic inhibitor Deposited 2003-01-02 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–256（256 aa）
Chain B 1–256（256 aa）
Mutation：A143Q Mutation：A143Q 0FP N-(6-aminohexanoyl)-3-methyl-L-valyl-3-methyl-L-valyl-N~1~-[(2S,3S)-3-hydroxy-4-oxo-4-{[(1R)-1-phenylpropyl]amino}butan-2-yl]-N~4~,N~4~-dimethyl-L-aspartamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；PEG 4000, HEPES, EDTA, Sodium Chloride, Sodium Sulfate, DTT, Spermine_HCl, Glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.70 Å R-free 0.273
1NJU Complex structure of HCMV Protease and a peptidomimetic inhibitor Deposited 2003-01-02 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 1–256（256 aa）
Chain D 1–256（256 aa）
Mutation：A143Q Mutation：A143Q 0FP N-(6-aminohexanoyl)-3-methyl-L-valyl-3-methyl-L-valyl-N~1~-[(2S,3S)-3-hydroxy-4-oxo-4-{[(1R)-1-phenylpropyl]amino}butan-2-yl]-N~4~,N~4~-dimethyl-L-aspartamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；PEG 4000, HEPES, EDTA, Sodium Chloride, Sodium Sulfate, DTT, Spermine_HCl, Glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.70 Å R-free 0.273
1NJU Complex structure of HCMV Protease and a peptidomimetic inhibitor Deposited 2003-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–256（256 aa）
Chain B 1–256（256 aa）
Chain C 1–256（256 aa）
Chain D 1–256（256 aa）
Mutation：A143Q Mutation：A143Q Mutation：A143Q Mutation：A143Q 0FP N-(6-aminohexanoyl)-3-methyl-L-valyl-3-methyl-L-valyl-N~1~-[(2S,3S)-3-hydroxy-4-oxo-4-{[(1R)-1-phenylpropyl]amino}butan-2-yl]-N~4~,N~4~-dimethyl-L-aspartamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；PEG 4000, HEPES, EDTA, Sodium Chloride, Sodium Sulfate, DTT, Spermine_HCl, Glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.70 Å R-free 0.273
1NKK COMPLEX STRUCTURE OF HCMV PROTEASE AND A PEPTIDOMIMETIC INHIBITOR Deposited 2003-01-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–256（256 aa） Fragment：Assemblin
Chain B 1–256（256 aa） Fragment：Assemblin
Mutation：A143Q, E31R Mutation：A143Q, E31R No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；PEG 4000, HEPES, EDTA, Sodium Chloride, Sodium Sulfate, DTT, Spermine_HCl, Glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.280
1NKK COMPLEX STRUCTURE OF HCMV PROTEASE AND A PEPTIDOMIMETIC INHIBITOR Deposited 2003-01-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–256（256 aa） Fragment：Assemblin
Chain D 1–256（256 aa） Fragment：Assemblin
Mutation：A143Q, E31R Mutation：A143Q, E31R No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；PEG 4000, HEPES, EDTA, Sodium Chloride, Sodium Sulfate, DTT, Spermine_HCl, Glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.280
1NKM Complex structure of HCMV Protease and a peptidomimetic inhibitor Deposited 2003-01-03 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–256（256 aa）
Chain B 1–256（256 aa）
Mutation：A143Q Mutation：A143Q 0FP N-(6-aminohexanoyl)-3-methyl-L-valyl-3-methyl-L-valyl-N~1~-[(2S,3S)-3-hydroxy-4-oxo-4-{[(1R)-1-phenylpropyl]amino}butan-2-yl]-N~4~,N~4~-dimethyl-L-aspartamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；PEG 4000, HEPES, EDTA, Sodium Chloride, Sodium Sulfate, DTT, Spermine_HCl, Glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.70 Å R-free 0.298
2WPO HCMV protease inhibitor complex Deposited 1998-08-04 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–256（256 aa）
Chain B 1–256（256 aa）
Mutation：A143Q, T181M, L229M Mutation：A143Q, T181M, L229M 01E (2S)-2-(3,3-dimethylbutanoylamino)-N-[(2S)-1-[[(2S,3S)-3-hydroxy-4-[(4-iodophenyl)methylamino]-4-oxo-butan-2-yl]amino]- 1,4-dioxo-4-pyrrol-1-yl-butan-2-yl]-3,3-dimethyl-butanamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 2.70 Å R-free 0.332
2WPO HCMV protease inhibitor complex Deposited 1998-08-04 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 1–256（256 aa）
Chain D 1–256（256 aa）
Mutation：A143Q, T181M, L229M Mutation：A143Q, T181M, L229M 01E (2S)-2-(3,3-dimethylbutanoylamino)-N-[(2S)-1-[[(2S,3S)-3-hydroxy-4-[(4-iodophenyl)methylamino]-4-oxo-butan-2-yl]amino]- 1,4-dioxo-4-pyrrol-1-yl-butan-2-yl]-3,3-dimethyl-butanamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 2.70 Å R-free 0.332
9Y7L HCMV Protease in complex with Fab5 - Class 1 Deposited 2025-09-10 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 × 3 PDB declaration: trimeric
Chain A 1–256（256 aa）
Mutation：A143V, A209V No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8；25 mM potassium phosphate, 150 mM potassium chloride, pH 8.0
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.70 Å
9Y7M HCMV Protease in complex with Fab5 - Class 2 Deposited 2025-09-10 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 × 3 PDB declaration: trimeric
Chain A 1–256（256 aa）
Mutation：A143V, A209V No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8；25 mM potassium phosphate, 150 mM potassium chloride, pH 8.0
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.57 Å
9Y7N HCMV Protease in complex with Fab5 - Class 3 Deposited 2025-09-10 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 × 3 PDB declaration: trimeric
Chain A 1–256（256 aa）
Mutation：A143V, A209V No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8；25 mM potassium phosphate, 150 mM potassium chloride, pH 8.0
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.69 Å

17 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VP40_HCMVA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–256； UniProt 1–256 Author chain B； PDBConstruct 1–256； UniProt 1–256

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 1wpo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1wpo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1wpo
Deposition date deposition_date1996-07-23
Structure title titleHYDROLYTIC ENZYME HUMAN CYTOMEGALOVIRUS PROTEASE
Keywords keywordsCOAT PROTEIN, HYDROLASE, SERINE PROTEASE, PHOSPHORYLATION, VIRAL PROTEASE, Viral protein; Viral protein, hydrolase
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_guinier24.90 Å
Radius of gyration Rg (electron density) rg_electron24.04 Å
Forward intensity I(0) i038551300.00
Molecular weight molecular_weight46974.0 kDa
Excluded volume excluded_volume58346 ų
Envelope volume envelope_volume68811 ų
Hydration-shell volume shell_volume24634 ų
Envelope diameter envelope_diameter85.7 Å
Shell Rg shell_rg30.64 Å
Envelope Rg envelope_rg24.35 Å
Shape Rg shape_rg24.06 Å
Total Rg total_rg24.71 Å
Total atoms total_atoms3290
Residues n_residues413
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 dmax83.8 Å
Rg (real space) rg_real25.05 Å
Rg uncertainty (real space) rg_real_error0.65 Å
I(0) (real space) i0_real3.8550e+07
I(0) uncertainty (real space) i0_real_error5.2370e+05
Rg (reciprocal space) rg_reciprocal25.02 Å
I(0) (reciprocal space) i0_reciprocal38550000.0000
Solution quality estimate total_estimate0.8459
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.3 Å
Skewness Skewness skewness0.505
Kurtosis Kurtosis kurtosis-0.268
Angular range angular_range— – 0.3200 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14590000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.762; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.875; Smooth: 0.833
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1wpoa_
Class classb — All beta proteins
Fold Fold foldb.57 — Herpes virus serine proteinase, assemblin
Superfamily Superfamily superfamilyb.57.1 — Herpes virus serine proteinase, assemblin
Family Family familyb.57.1.1 — Herpes virus serine proteinase, assemblin
Domain ID domain_idd1wpob_
Class classb — All beta proteins
Fold Fold foldb.57 — Herpes virus serine proteinase, assemblin
Superfamily Superfamily superfamilyb.57.1 — Herpes virus serine proteinase, assemblin
Family Family familyb.57.1.1 — Herpes virus serine proteinase, assemblin

CATH v4.4 (2 domains)

Domain ID domain_id1wpoA00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology16 — Serine Protease, Human Cytomegalovirus Protease; Chain A
Homologous superfamily homologous superfamily10 — Herpesvirus/Caudovirus protease domain
Domain ID domain_id1wpoB00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology16 — Serine Protease, Human Cytomegalovirus Protease; Chain A
Homologous superfamily homologous superfamily10 — Herpesvirus/Caudovirus protease domain
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8. Citations (1)

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9. Files and Curves (10)