1avo

PROTEASOME ACTIVATOR REG(ALPHA)

Method: X-RAY DIFFRACTION

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

11S REGULATOR

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 14	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PSME1_HUMAN
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–60； UniProt 4–63 Author chain C； PDBConstruct 1–60； UniProt 4–63 Author chain E； PDBConstruct 1–60； UniProt 4–63 Author chain G； PDBConstruct 1–60； UniProt 4–63 Author chain I； PDBConstruct 1–60； UniProt 4–63 Author chain K； PDBConstruct 1–60； UniProt 4–63 Author chain M； PDBConstruct 1–60； UniProt 4–63 Author chain B； PDBConstruct 2–140； UniProt 104–242 Author chain D； PDBConstruct 2–140； UniProt 104–242 Author chain F； PDBConstruct 2–140； UniProt 104–242 Author chain H； PDBConstruct 2–140； UniProt 104–242 Author chain J； PDBConstruct 2–140； UniProt 104–242 Author chain L； PDBConstruct 2–140； UniProt 104–242 Author chain N； PDBConstruct 2–140； UniProt 104–242

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	1avo
Deposition date deposition_date	1997-09-18
Structure title title	PROTEASOME ACTIVATOR REG(ALPHA)
Keywords keywords	PROTEASOME ACTIVATOR, CELL ADHESION, INTERFERON INDUCTION; PROTEASOME ACTIVATOR
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.

1avo__assembly_1__model_1

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

Download this curve (.dat)

1avo__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1avo__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	35.69 Å
Rg (electron density)	34.31 Å
Total Rg	35.05 Å
Atom count	11361
Residues	1400
Excluded volume	204510 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1avo__assembly_1__model_1`	tetradecameric （14）	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)

Entity 1 Entity 1 polymer

Description description	11S REGULATOR
Molecular weight formula_weight	6753.7 kDa
Source method src_method	man
Copy count entity_count	7

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E,G,I,K,M
Atom count atom_count	11361

LRVQPEAQAKVDVFREDLCTKTENLLGSYFPKKISELDAFLKEPALNEANLSNLKAPLDI

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	11S REGULATOR
Molecular weight formula_weight	16318.9 kDa
Source method src_method	man
Copy count entity_count	7

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F,H,J,L,N

AVNCNEKIVVLLQRLKPEIKDVIEQLNLVTTWLQLQIPRIEDGNNFGVAVQEKVFELMTSLHTKLEGFHTQISKYFSERGDAVTKAAKQPHVGDYRQLVHELDEAEYRDIRLMVMEIRNAYAVLYDIILKNFEKLKKPRG

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli BL21(DE3)

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6. Fold Classification (SCOP + CATH) 21 domains

SCOP 2.08 (7 domains)

Domain ID domain_id	d1avo.1
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.8 — Proteasome activator
Family Family family	a.24.8.1 — Proteasome activator

Domain ID domain_id	d1avo.2
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.8 — Proteasome activator
Family Family family	a.24.8.1 — Proteasome activator

Domain ID domain_id	d1avo.3
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.8 — Proteasome activator
Family Family family	a.24.8.1 — Proteasome activator

Domain ID domain_id	d1avo.4
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.8 — Proteasome activator
Family Family family	a.24.8.1 — Proteasome activator

Domain ID domain_id	d1avo.5
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.8 — Proteasome activator
Family Family family	a.24.8.1 — Proteasome activator

Domain ID domain_id	d1avo.6
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.8 — Proteasome activator
Family Family family	a.24.8.1 — Proteasome activator

Domain ID domain_id	d1avo.7
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.8 — Proteasome activator
Family Family family	a.24.8.1 — Proteasome activator

CATH v4.4 (14 domains)

Domain ID domain_id	1avoA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	120 — Proteasome activator pa28, N-terminal domain

Domain ID domain_id	1avoB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	180 — Proteasome activator pa28, C-terminal domain

Domain ID domain_id	1avoC00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	120 — Proteasome activator pa28, N-terminal domain

Domain ID domain_id	1avoD00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	180 — Proteasome activator pa28, C-terminal domain

Domain ID domain_id	1avoE00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	120 — Proteasome activator pa28, N-terminal domain

Domain ID domain_id	1avoF00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	180 — Proteasome activator pa28, C-terminal domain

Domain ID domain_id	1avoG00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	120 — Proteasome activator pa28, N-terminal domain

Domain ID domain_id	1avoH00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	180 — Proteasome activator pa28, C-terminal domain

Domain ID domain_id	1avoI00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	120 — Proteasome activator pa28, N-terminal domain

Domain ID domain_id	1avoJ00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	180 — Proteasome activator pa28, C-terminal domain

Domain ID domain_id	1avoK00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	120 — Proteasome activator pa28, N-terminal domain

Domain ID domain_id	1avoL00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	180 — Proteasome activator pa28, C-terminal domain

Domain ID domain_id	1avoM00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	120 — Proteasome activator pa28, N-terminal domain

Domain ID domain_id	1avoN00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	180 — Proteasome activator pa28, C-terminal domain

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Unit-cell length a length_a	162.600 Å
Unit-cell length b length_b	134.300 Å
Unit-cell length c length_c	116.200 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.60 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	28

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.2490
R_work r_work	0.2490
R_free r_free	0.2890

PROTEASOME ACTIVATOR REG(ALPHA)

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

11S REGULATOR

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

1avo__assembly_1__model_1

1avo__assembly_1__model_1 | I(q)

1avo__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 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 21 domains

SCOP 2.08 (7 domains)

CATH v4.4 (14 domains)

7. Citations (1)

PROTEASOME ACTIVATOR REG(ALPHA)

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

11S REGULATOR

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

1avo__assembly_1__model_1

1avo__assembly_1__model_1 | I(q)

1avo__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 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 21 domains

SCOP 2.08 (7 domains)

CATH v4.4 (14 domains)

7. Citations (1)