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7jre

Crystal structure of EV-D68 2A protease C107A mutant

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Protease 2A

Human enterovirus D68

UniProt A0A097BW19

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 ZINC ION × 2 water × 2 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 2 ZINC ION × 2 water × 2 Consistent with protein count
3 Protein homooligomer Homooligomer Protein 2 ZINC ION × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
7lw2 7lw2 7lw2 7lw2 7lw2 7lw2 7mg0 7mg0 7mg0 7mg0 7mg0 7mg0

12 assemblies

Homodimer
7jre 7jre 7jre

3 assemblies

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex
9c4a 9c4a 9c4a 9c4a 9c4a 9c8g 9c8g 9c8g 9c8g 9c8g 9c8h 9c8h

15 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name A0A097BW19_HED68
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–147； UniProt 863–1009 Author chain B； PDBConstruct 1–147； UniProt 863–1009 Author chain C； PDBConstruct 1–147； UniProt 863–1009 Author chain D； PDBConstruct 1–147； UniProt 863–1009 Author chain E； PDBConstruct 1–147； UniProt 863–1009 Author chain F； PDBConstruct 1–147； UniProt 863–1009

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id7jre
Deposition date deposition_date2020-08-12
Structure title titleCrystal structure of EV-D68 2A protease C107A mutant
Keywords keywords;metal ion binding, viral process, Enterovirus EV-D68, protease, catalytic activity, ion binding, structural molecule activity, modulation of process of other organism, interaction with host, cellular process, gene expression, regulation of biological process, biological regulation, VIRAL PROTEIN, HYDROLASE ;; VIRAL PROTEIN, HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

7jre__assembly_3__model_1

Assembly 3 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

7jre__assembly_3__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

7jre__assembly_3__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）20.19 Å
Rg (electron density)19.58 Å
Total Rg20.18 Å
Atom count3951
Residues279
Excluded volume36449 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 7jre__assembly_1__model_1 dimeric （2） Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 7jre__assembly_2__model_1 dimeric （2） Success 4.1.3-1-20251215 (887e7ef) View Download
3 1 7jre__assembly_3__model_1 dimeric （2） Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

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7. Citations (1)