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9c7w

human OC43 Main Protease (1-303) in complex with potent inhibitor

Method: X-RAY DIFFRACTION Dmax: 107.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ORF1ab polyprotein

Human coronavirus OC43

UniProt U3M6R3

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 3247–3544 Mutation：P3460L A1AUY (8S)-3-(4,4-difluorocyclohexyl)-5-(pyrimidin-2-yl)pyrazolo[1,5-a]pyrimidine × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；0.1M HEPES pH 7.5, 8% EG, 10% PEG 8K Resolution 2.08 Å R-free 0.246
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 3247–3544 Mutation：P3460L A1AUY (8S)-3-(4,4-difluorocyclohexyl)-5-(pyrimidin-2-yl)pyrazolo[1,5-a]pyrimidine × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；0.1M HEPES pH 7.5, 8% EG, 10% PEG 8K Resolution 2.08 Å R-free 0.246
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain C； UniProt 3247–3544 Mutation：P3460L A1AUY (8S)-3-(4,4-difluorocyclohexyl)-5-(pyrimidin-2-yl)pyrazolo[1,5-a]pyrimidine × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；0.1M HEPES pH 7.5, 8% EG, 10% PEG 8K Resolution 2.08 Å R-free 0.246
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain D； UniProt 3247–3544 Mutation：P3460L A1AUY (8S)-3-(4,4-difluorocyclohexyl)-5-(pyrimidin-2-yl)pyrazolo[1,5-a]pyrimidine × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；0.1M HEPES pH 7.5, 8% EG, 10% PEG 8K Resolution 2.08 Å R-free 0.246

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 9C7W Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
9PAE Crystal structure of HCoV OC43 3CLpro with ALG-097608 (inhibitor 1) Deposited 2025-06-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3247–3549（303 aa）
Chain B 3247–3549（303 aa）
Not recorded A1CHF (1R,2R,3S,6S,7S)-4-[(2S)-3,3-dimethyl-2-(2,2,2-trifluoroacetamido)butanoyl]-10,10-difluoro-N-{(1E,2R)-1-imino-3-[(3R)-2-oxo-3,4-dihydro-2H-pyrrol-3-yl]propan-2-yl}-4-azatricyclo[5.2.1.0~2,6~]decane-3-carboxamide (non-preferred name) × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.2M Potassium thiocyanate, 0.1 M Bis-Tris pH 8.5 and 20% PEG3350
Resolution 2.31 Å R-free 0.280
9PAE Crystal structure of HCoV OC43 3CLpro with ALG-097608 (inhibitor 1) Deposited 2025-06-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 3247–3549（303 aa）
Chain D 3247–3549（303 aa）
Not recorded A1CHF (1R,2R,3S,6S,7S)-4-[(2S)-3,3-dimethyl-2-(2,2,2-trifluoroacetamido)butanoyl]-10,10-difluoro-N-{(1E,2R)-1-imino-3-[(3R)-2-oxo-3,4-dihydro-2H-pyrrol-3-yl]propan-2-yl}-4-azatricyclo[5.2.1.0~2,6~]decane-3-carboxamide (non-preferred name) × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.2M Potassium thiocyanate, 0.1 M Bis-Tris pH 8.5 and 20% PEG3350
Resolution 2.31 Å R-free 0.280
9Y8X OC43 Mpro with EGT710 Deposited 2025-09-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3247–3549（303 aa）
Not recorded A1CBU (4S)-4-(iminomethyl)-3-(isoquinolin-4-yl)-1-[6-(trifluoromethyl)pyridin-3-yl]imidazolidin-2-one × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；294 K；0.2M NaSCN, 30% Peg 3350
Resolution 2.12 Å R-free 0.265

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name U3M6R3_CVHOC
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–298； UniProt 3247–3544 Author chain B； PDBConstruct 1–298； UniProt 3247–3544 Author chain C； PDBConstruct 1–298； UniProt 3247–3544 Author chain D； PDBConstruct 1–298； UniProt 3247–3544

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 9c7w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9c7w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9c7w
Deposition date deposition_date2024-06-11
Structure title titlehuman OC43 Main Protease (1-303) in complex with potent inhibitor
Keywords keywordsmain protease, hydrolase, OC43, protease, peptidase, 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_guinier34.68 Å
Radius of gyration Rg (electron density) rg_electron33.99 Å
Forward intensity I(0) i0258164000.00
Molecular weight molecular_weight130680.0 kDa
Excluded volume excluded_volume163750 ų
Envelope volume envelope_volume206120 ų
Hydration-shell volume shell_volume50354 ų
Envelope diameter envelope_diameter115.1 Å
Shell Rg shell_rg40.90 Å
Envelope Rg envelope_rg33.60 Å
Shape Rg shape_rg33.97 Å
Total Rg total_rg34.55 Å
Total atoms total_atoms9218
Residues n_residues1192
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 dmax107.5 Å
Rg (real space) rg_real34.58 Å
Rg uncertainty (real space) rg_real_error0.66 Å
I(0) (real space) i0_real2.5820e+08
I(0) uncertainty (real space) i0_real_error3.7620e+06
Rg (reciprocal space) rg_reciprocal34.64 Å
I(0) (reciprocal space) i0_reciprocal258200000.0000
Solution quality estimate total_estimate0.8882
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.4 Å
Skewness Skewness skewness0.249
Kurtosis Kurtosis kurtosis-0.348
Angular range angular_range— – 0.2300 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35280000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.923; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.784
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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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8. Citations (1)

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9. Files and Curves (10)