4x2y

Crystal structure of a chimeric Murine Norovirus NS6 protease (inactive C139A mutant) in which the P4-P4 prime residues of the cleavage junction in the extended C-terminus have been replaced by the corresponding residues from the NS2-3 junction.

Method: X-RAY DIFFRACTION

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

NS6 Protease,NS6 Protease

Murine norovirus 1

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q80J95_9CALI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–176； UniProt 998–1173 Author chain A； PDBConstruct 177–179； UniProt 338–340 Author chain B； PDBConstruct 1–176； UniProt 998–1173 Author chain B； PDBConstruct 177–179； UniProt 338–340

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_id	4x2y
Deposition date deposition_date	2014-11-27
Structure title title	Crystal structure of a chimeric Murine Norovirus NS6 protease (inactive C139A mutant) in which the P4-P4 prime residues of the cleavage junction in the extended C-terminus have been replaced by the corresponding residues from the NS2-3 junction.
Keywords keywords	Murine norovirus, Protease, viral protein; VIRAL PROTEIN
Experimental Method method	X-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.

4x2y__assembly_1__model_1

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

Download this curve (.dat)

4x2y__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4x2y__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	17.03 Å
Rg (electron density)	15.72 Å
Total Rg	16.93 Å
Atom count	1273
Residues	172
Excluded volume	22782 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4x2y__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`4x2y__assembly_2__model_1`	monomeric （1）	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 (2)

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d4x2ya_
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.4 — Viral cysteine protease of trypsin fold

Domain ID domain_id	d4x2yb_
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.4 — Viral cysteine protease of trypsin fold

CATH v4.4 (4 domains)

Domain ID domain_id	4x2yA01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	4x2yA02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	4x2yB01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	4x2yB02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

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Unit-cell length a length_a	35.520 Å
Unit-cell length b length_b	47.320 Å
Unit-cell length c length_c	53.070 Å
Unit-cell angle α angle_alpha	104.45 °
Unit-cell angle β angle_beta	91.53 °
Unit-cell angle γ angle_gamma	110.61 °
Molecules per unit cell Z z_pdb	2

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.417 Å
Low-resolution limit resolution_low	19.273 Å
R factor r_factor	0.2129
R_work r_work	0.2104
R_free r_free	0.2616

Description description	NS6 Protease,NS6 Protease
Molecular weight formula_weight	18824.5 kDa
Mutation mutation	C139A,C139A
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2669

Crystal structure of a chimeric Murine Norovirus NS6 protease (inactive C139A mutant) in which the P4-P4 prime residues of the cleavage junction in the extended C-terminus have been replaced by the corresponding residues from the NS2-3 junction.

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

NS6 Protease,NS6 Protease

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

4x2y__assembly_1__model_1

4x2y__assembly_1__model_1 | I(q)

4x2y__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (2)

Source organism organism	Murine norovirus 1
NCBI taxonomy ID ncbi_taxonomy_id	223997
Host organism host_organism	Escherichia coli BL21(DE3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	107

Crystal structure of a chimeric Murine Norovirus NS6 protease (inactive C139A mutant) in which the P4-P4 prime residues of the cleavage junction in the extended C-terminus have been replaced by the corresponding residues from the NS2-3 junction.

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

NS6 Protease,NS6 Protease

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

4x2y__assembly_1__model_1

4x2y__assembly_1__model_1 | I(q)

4x2y__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (2)