SAXSdb — 2wpo

▼

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

HUMAN CYTOMEGALOVIRUS PROTEASE

Human herpesvirus 5

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	;(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	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	;(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	Consistent with protein count

Other States of the Same Protein in the Database

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 Author chain C； PDBConstruct 1–256； UniProt 1–256 Author chain D； 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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	2wpo
Deposition date deposition_date	1998-08-04
Structure title title	HCMV protease inhibitor complex
Keywords keywords	VIRAL PROTEASE, HYDROLASE-HYDROLASE INHIBITOR complex, COAT PROTEIN, SERINE PROTEASE; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method method	X-RAY DIFFRACTION

▼

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.

2wpo__assembly_1__model_1

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

Download this curve (.dat)

2wpo__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2wpo__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	25.25 Å
Rg (electron density)	24.29 Å
Total Rg	24.97 Å
Atom count	4536
Residues	460
Excluded volume	64812 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2wpo__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2wpo__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	HUMAN CYTOMEGALOVIRUS PROTEASE
Molecular weight formula_weight	28178.7 kDa
EC 编号 ec_number	3.4.21.-
Mutation mutation	A143Q, T181M, L229M
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	9072

MTMDEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWLHAQGQGQPSLSVALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPRFLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSLSSRRCDDVEQATSLSGSETTPFKHVALCSVGRRRGTLAVYGRDPEWVMQRFPDLTAADRDGLRAQWQRCGSTAVDASGDPFRSDSYGLLGNSVDAMYIRERLPKLRYDKQLVGVTERESYVKA

Source Source

Source organism organism	Human herpesvirus 5
Common name common_name	Human cytomegalovirus
NCBI taxonomy ID ncbi_taxonomy_id	10359
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	;(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 ;
Molecular weight formula_weight	709.6 kDa
Source method src_method	syn
Copy count entity_count	4

▼

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2wpoa_
Class class	b — All beta proteins
Fold Fold fold	b.57 — Herpes virus serine proteinase, assemblin
Superfamily Superfamily superfamily	b.57.1 — Herpes virus serine proteinase, assemblin
Family Family family	b.57.1.1 — Herpes virus serine proteinase, assemblin

Domain ID domain_id	d2wpob_
Class class	b — All beta proteins
Fold Fold fold	b.57 — Herpes virus serine proteinase, assemblin
Superfamily Superfamily superfamily	b.57.1 — Herpes virus serine proteinase, assemblin
Family Family family	b.57.1.1 — Herpes virus serine proteinase, assemblin

Domain ID domain_id	d2wpoc_
Class class	b — All beta proteins
Fold Fold fold	b.57 — Herpes virus serine proteinase, assemblin
Superfamily Superfamily superfamily	b.57.1 — Herpes virus serine proteinase, assemblin
Family Family family	b.57.1.1 — Herpes virus serine proteinase, assemblin

Domain ID domain_id	d2wpod_
Class class	b — All beta proteins
Fold Fold fold	b.57 — Herpes virus serine proteinase, assemblin
Superfamily Superfamily superfamily	b.57.1 — Herpes virus serine proteinase, assemblin
Family Family family	b.57.1.1 — Herpes virus serine proteinase, assemblin

CATH v4.4 (4 domains)

Domain ID domain_id	2wpoA00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	16 — Serine Protease, Human Cytomegalovirus Protease; Chain A
Homologous superfamily homologous superfamily	10 — Herpesvirus/Caudovirus protease domain

Domain ID domain_id	2wpoB00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	16 — Serine Protease, Human Cytomegalovirus Protease; Chain A
Homologous superfamily homologous superfamily	10 — Herpesvirus/Caudovirus protease domain

Domain ID domain_id	2wpoC00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	16 — Serine Protease, Human Cytomegalovirus Protease; Chain A
Homologous superfamily homologous superfamily	10 — Herpesvirus/Caudovirus protease domain

Domain ID domain_id	2wpoD00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	16 — Serine Protease, Human Cytomegalovirus Protease; Chain A
Homologous superfamily homologous superfamily	10 — Herpesvirus/Caudovirus protease domain

▶

Unit-cell length a length_a	107.800 Å
Unit-cell length b length_b	53.400 Å
Unit-cell length c length_c	212.400 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

Space group space_group	P 21 2 21
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	6.000 Å
R factor r_factor	0.2260
R_work r_work	0.2260
R_free r_free	0.3320

HCMV protease inhibitor complex

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

HUMAN CYTOMEGALOVIRUS 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

2wpo__assembly_1__model_1

2wpo__assembly_1__model_1 | I(q)

2wpo__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 non-polymer

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (2)

HCMV protease inhibitor complex

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

HUMAN CYTOMEGALOVIRUS 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

2wpo__assembly_1__model_1

2wpo__assembly_1__model_1 | I(q)

2wpo__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 non-polymer

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (2)