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9zjb

Crystal structure of MERS 3CL protease in complex with inhibitor IKR-I-46

Method: X-RAY DIFFRACTION Dmax: 76.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

3C-like proteinase nsp5

Middle East respiratory syndrome-related coronavirus

UniProt K9N638

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 3248–3553 Fragment：UNP residues 3248-3553 CALCIUM ION × 2 ;N~2~-[(2S,4S)-3-benzyl-4-methyl-2-oxo-1,3,2lambda~5~-oxazaphospholidin-2-yl]-N-{(2S)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-leucinamide ; × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.88 Å R-free 0.216

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 9ZJB Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4R3D Crystal structure of MERS Coronavirus papain like protease Deposited 2014-08-15 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1481–1811（331 aa） Fragment：UNP RESIDUES 1481-1811
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；0.1M sodium chloride, 0.1M HEPES (pH 7.0), 1.6M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.82 Å R-free 0.224
4R3D Crystal structure of MERS Coronavirus papain like protease Deposited 2014-08-15 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1481–1811（331 aa） Fragment：UNP RESIDUES 1481-1811
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；0.1M sodium chloride, 0.1M HEPES (pH 7.0), 1.6M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.82 Å R-free 0.224
7T3Y Structure of MERS 3CL protease in complex with inhibitor 8c Deposited 2021-12-09 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 3248–3553（306 aa） Fragment：Full Length
Chain B 3248–3553（306 aa） Fragment：Full Length
Not recorded F5L (1R,2S)-1-hydroxy-2-{[N-({[7-(2-methylpropanoyl)-7-azaspiro[3.5]nonan-2-yl]oxy}carbonyl)-L-leucyl]amino}-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 F8C (1S,2S)-1-hydroxy-2-{[N-({[7-(2-methylpropanoyl)-7-azaspiro[3.5]nonan-2-yl]oxy}carbonyl)-L-leucyl]amino}-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；20% (w/v) PEG 3350, 100 mM, 200 mM ammonium sulfate
Resolution 1.90 Å R-free 0.258
7T3Z Structure of MERS 3CL protease in complex with inhibitor 9c Deposited 2021-12-09 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 3248–3553（306 aa） Fragment：Full Length
Chain B 3248–3553（306 aa） Fragment：Full Length
Not recorded FHS (1S,2S)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]-2-{[N-({[7-(phenylacetyl)-7-azaspiro[3.5]nonan-2-yl]oxy}carbonyl)-L-leucyl]amino}propane-1-sulfonic acid × 2 FEY (1R,2S)-2-{[N-({[(2r,4R)-7-acetyl-7-azaspiro[3.5]non-5-en-2-yl]oxy}carbonyl)-L-leucyl]amino}-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；30% (w/v) PEG 550 MME, 100 mM, 50 mM magnesium chloride
Resolution 1.95 Å R-free 0.206
7T40 Structure of MERS 3CL protease in complex with inhibitor 10c Deposited 2021-12-09 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3248–3553（306 aa） Fragment：Full Length
Not recorded FV5 (1R,2S)-1-hydroxy-2-{[N-({[7-(methanesulfonyl)-7-azaspiro[3.5]nonan-2-yl]oxy}carbonyl)-L-leucyl]amino}-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 FVE (1S,2S)-1-hydroxy-2-{[N-({[7-(methanesulfonyl)-7-azaspiro[3.5]nonan-2-yl]oxy}carbonyl)-L-leucyl]amino}-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 PG4 TETRAETHYLENE GLYCOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；17% (w/v) PEG 10000, 100 mM Bis-Tris, 100 mM ammonium acetate
Resolution 1.70 Å R-free 0.195
7T41 Structure of MERS 3CL protease in complex with inhibitor 14c Deposited 2021-12-09 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3248–3553（306 aa） Fragment：Full Length
Not recorded FWI (1R,2S)-2-{[N-({[1-(tert-butoxycarbonyl)azetidin-3-yl]methoxy}carbonyl)-L-leucyl]amino}-1-hydroxy-3-[(3R)-2-oxo-2,3-dihydro-1H-pyrrol-3-yl]propane-1-sulfonic acid × 2 FZI (1S,2S)-2-{[N-({[1-(tert-butoxycarbonyl)azetidin-3-yl]methoxy}carbonyl)-L-leucyl]amino}-1-hydroxy-3-[(3R)-2-oxo-2,3-dihydro-1H-pyrrol-3-yl]propane-1-sulfonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；25% (w/v) PEG 3350, 100 mM Hepes, 200 mM magnesium chloride
Resolution 2.10 Å R-free 0.237
8R5J Crystal structure of MERS-CoV main protease Deposited 2023-11-16 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3248–3553（306 aa）
Chain B 3248–3553（306 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2M Sodium malonate dibasic monohydrate, 20% w/v PEG 3350
Resolution 1.90 Å R-free 0.242
9ATA Crystal structure of MERS 3CL protease in complex with a phenylethyl 2-pyrrolidone inhibitor Deposited 2024-02-26 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 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Chain B 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Not recorded A1AGG (1S,2S)-1-hydroxy-2-{[N-({[(2S)-5-oxo-1-(2-phenylethyl)pyrrolidin-2-yl]methoxy}carbonyl)-L-leucyl]amino}-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 A1AGH (1R,2S)-1-hydroxy-2-{[N-({[(2S)-5-oxo-1-(2-phenylethyl)pyrrolidin-2-yl]methoxy}carbonyl)-L-leucyl]amino}-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；30% w/v PEG2000 MME, 150 mM potassium bromide
Resolution 1.65 Å R-free 0.188
9ATD Crystal structure of MERS 3CL protease in complex with a ethylcyclohexyl 2-pyrrolidone inhibitor (S-enantiomer) inhibitor Deposited 2024-02-26 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Not recorded A1AGL (1S,2S)-2-{[N-({[(2S)-1-(2-cyclohexylethyl)-5-oxopyrrolidin-2-yl]methoxy}carbonyl)-L-leucyl]amino}-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 A1AGK (1R,2S)-2-{[N-({[(2S)-1-(2-cyclohexylethyl)-5-oxopyrrolidin-2-yl]methoxy}carbonyl)-L-leucyl]amino}-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；291 K；25% w/v PEG3350, 100 mM Bis-Tris, pH 5.5, 200 mM ammonium acetate
Resolution 1.80 Å R-free 0.201
9ATE Crystal structure of MERS 3CL protease in complex with a methylbicyclo[2.2.1]heptane 2-pyrrolidone inhibitor Deposited 2024-02-26 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 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Chain B 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Not recorded A1AGN (1S,2S)-2-{[N-({[(2S)-1-{[(1S,2S,4R)-bicyclo[2.2.1]heptan-2-yl]methyl}-5-oxopyrrolidin-2-yl]methoxy}carbonyl)-L-leucyl]amino}-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 A1AGM (1R,2S)-2-{[N-({[(2S)-1-{[(1S,2S,4R)-bicyclo[2.2.1]heptan-2-yl]methyl}-5-oxopyrrolidin-2-yl]methoxy}carbonyl)-L-leucyl]amino}-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；25% w/v PEG3350, 100 mM HEPES, pH 7.5
Resolution 1.85 Å R-free 0.191
9ATF Crystal structure of MERS 3CL protease in complex with a 1-methyl-4,4-difluorocyclohexyl 2-pyrrolidone inhibitor Deposited 2024-02-26 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Not recorded A1AGP (1S,2S)-2-({N-[({(2S)-1-[(4,4-difluorocyclohexyl)methyl]-5-oxopyrrolidin-2-yl}methoxy)carbonyl]-L-leucyl}amino)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 A1AGO (1R,2S)-2-({N-[({(2S)-1-[(4,4-difluorocyclohexyl)methyl]-5-oxopyrrolidin-2-yl}methoxy)carbonyl]-L-leucyl}amino)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；291 K；25% w/v PEG3350, 100 mM Bis-Tris, pH 5.5, 200 mM sodium chloride
Resolution 1.50 Å R-free 0.179
9ATG Crystal structure of MERS 3CL protease in complex with a 2,2-difluoro-5-methylbenzo[1,3]dioxole 2-pyrrolidone inhibitor Deposited 2024-02-26 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Not recorded A1AGT (1S,2S)-2-({N-[({(2S)-1-[(2,2-difluoro-2H-1,3-benzodioxol-5-yl)methyl]-5-oxopyrrolidin-2-yl}methoxy)carbonyl]-L-leucyl}amino)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 A1AGS (1R,2S)-2-({N-[({(2S)-1-[(2,2-difluoro-2H-1,3-benzodioxol-5-yl)methyl]-5-oxopyrrolidin-2-yl}methoxy)carbonyl]-L-leucyl}amino)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；25% w/v PEG3350, 100 mM Tris, pH 8.5, 200 mM magnesium chloride hexahydrate
Resolution 1.75 Å R-free 0.199
9ATH Crystal structure of MERS 3CL protease in complex with a methylbicyclo[2.2.1]heptene 2-pyrrolidone inhibitor Deposited 2024-02-26 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 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Chain B 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Not recorded A1AGR (1S,2S)-2-{[N-({[(2S)-1-{[(1R,2S,4R)-bicyclo[2.2.1]hept-5-en-2-yl]methyl}-5-oxopyrrolidin-2-yl]methoxy}carbonyl)-L-leucyl]amino}-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 A1AGQ (1R,2S)-2-{[N-({[(2S)-1-{[(1R,2S,4R)-bicyclo[2.2.1]hept-5-en-2-yl]methyl}-5-oxopyrrolidin-2-yl]methoxy}carbonyl)-L-leucyl]amino}-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；800 mM potassium sodium tartrate tetrahydrate, 100 mM Tris, pH 8.5, 0.5% w/v PEG5000 MME
Resolution 1.65 Å R-free 0.208
9ATI Crystal structure of MERS 3CL protease in complex with a racemic bicyclo[2.2.1]heptenyl-methyl 2-pyrrolidone inhibitor Deposited 2024-02-26 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Not recorded A1AGV (1S,2S)-2-{[N-({[(3S)-1-{[(1R,2R,4R)-bicyclo[2.2.1]hept-5-en-2-yl]methyl}-5-oxopyrrolidin-3-yl]methoxy}carbonyl)-L-leucyl]amino}-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 A1AGU (1R,2S)-2-{[N-({[(3S)-1-{[(1R,2R,4R)-bicyclo[2.2.1]hept-5-en-2-yl]methyl}-5-oxopyrrolidin-3-yl]methoxy}carbonyl)-L-leucyl]amino}-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；25% w/v PEG3350, 100 mM Tris, pH 8.5, 200 mM ammonium acetate
Resolution 1.60 Å R-free 0.196
9ATJ Crystal structure of MERS 3CL protease in complex with a m-chlorobenzyl 2-pyrrolidone inhibitor Deposited 2024-02-26 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Not recorded MG MAGNESIUM ION × 2 A1AGJ (1S,2S)-2-({N-[({(2S)-1-[(3-chlorophenyl)methyl]-5-oxopyrrolidin-2-yl}methoxy)carbonyl]-L-leucyl}amino)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 A1AGI (1R,2S)-2-({N-[({(2S)-1-[(3-chlorophenyl)methyl]-5-oxopyrrolidin-2-yl}methoxy)carbonyl]-L-leucyl}amino)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；291 K；15% v/v PEG400, 100 mM MES, pH 6.0, 100 mM calcium acetate
Resolution 1.40 Å R-free 0.170
9ATS Crystal structure of MERS 3CL protease in complex with a methylcyclohexyl 2-pyrrolidone inhibitor (S-enantiomer) Deposited 2024-02-27 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Not recorded A1AGX (1S,2S)-2-{[N-({[(2S)-1-(cyclohexylmethyl)-5-oxopyrrolidin-2-yl]methoxy}carbonyl)-L-leucyl]amino}-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；28% w/v PEG2000 MME, 100 mM Bis-Tris pH 6.5
Resolution 2.50 Å R-free 0.252
9ATT Crystal structure of MERS 3CL protease in complex with a methylcyclohexyl 2-pyrrolidone inhibitor (R-enantiomer) Deposited 2024-02-27 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 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Chain B 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Not recorded A1AGZ (1S,2S)-2-{[N-({[(2R)-1-(cyclohexylmethyl)-5-oxopyrrolidin-2-yl]methoxy}carbonyl)-L-leucyl]amino}-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 A1AGY (1R,2S)-2-{[N-({[(2R)-1-(cyclohexylmethyl)-5-oxopyrrolidin-2-yl]methoxy}carbonyl)-L-leucyl]amino}-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；10% w/v PEG3350, 100 mM HEPES, pH 7.5, 200 mM L-proline
Resolution 1.70 Å R-free 0.210
9BOO Crystal structure of MERS-CoV Nsp5 in complex with PF-07817883 Deposited 2024-05-05 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3248–3553（306 aa） Fragment：residues 3248-3553
Not recorded YDL N-(methoxycarbonyl)-3-methyl-L-valyl-(4R)-N-{(1Z,2S)-1-imino-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-4-(trifluoromethyl)-L-prolinamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291.15 K；0.2 M Magnesium chloride hexahydrate, 0.1 M HEPES 7.0, 20 % w/v PEG 6000
Resolution 1.50 Å R-free 0.195
9N9V Main protease of MERS in complex with AVI8122 Deposited 2025-02-11 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 3248–3550（303 aa）
Chain B 3248–3550（303 aa）
Not recorded A1BWH N-[(2S)-3-cyclopropyl-1-({(2S,3S)-3,4-dihydroxy-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl}amino)-1-oxopropan-2-yl]-7-fluoro-1H-indole-2-carboxamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291.15 K；8% PEG 8K, 0.1 M Tris-HCl pH 7.5
Resolution 2.50 Å R-free 0.287
9ZJ8 Crystal structure of MERS 3CL protease in complex with inhibitor AMJ-II-72 Deposited 2025-12-04 Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.10 Å R-free 0.247
9ZJC Crystal structure of MERS 3CL protease in complex with inhibitor IKR-I-52 Deposited 2025-12-04 Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3248–3553（306 aa） Fragment：UNP residues 3248-3553
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.90 Å R-free 0.223

20 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name R1A_MERS1
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 8–313； UniProt 3248–3553

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 9zjb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9zjb
Deposition date deposition_date2025-12-04
最后修订 last_revision2026-06-10
Structure title titleCrystal structure of MERS 3CL protease in complex with inhibitor IKR-I-46
Keywords keywordsHYDROLASE, HYDROLASE-HYDROLASE INHIBITOR complex; HYDROLASE/HYDROLASE INHIBITOR
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_guinier22.08 Å
Radius of gyration Rg (electron density) rg_electron21.61 Å
Forward intensity I(0) i036054000.00
Molecular weight molecular_weight31003.0 kDa
Excluded volume excluded_volume29969 ų
Envelope volume envelope_volume48207 ų
Hydration-shell volume shell_volume19538 ų
Envelope diameter envelope_diameter75.9 Å
Shell Rg shell_rg27.17 Å
Envelope Rg envelope_rg21.72 Å
Shape Rg shape_rg21.63 Å
Total Rg total_rg22.14 Å
Total atoms total_atoms2328
Residues n_residues305
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 dmax76.1 Å
Rg (real space) rg_real22.21 Å
Rg uncertainty (real space) rg_real_error0.48 Å
I(0) (real space) i0_real3.6050e+07
I(0) uncertainty (real space) i0_real_error4.8990e+05
Rg (reciprocal space) rg_reciprocal22.19 Å
I(0) (reciprocal space) i0_reciprocal36050000.0000
Solution quality estimate total_estimate0.8435
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.6 Å
Skewness Skewness skewness0.466
Kurtosis Kurtosis kurtosis-0.387
Angular range angular_range— – 0.3600 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9978000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.743; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.782; Smooth: 0.951
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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8. Citations (1)

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9. Files and Curves (10)