SAXSdb — 1vq0

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

33 kDa chaperonin

Thermotoga maritima

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 CHLORIDE ION × 2 UNKNOWN LIGAND × 2 1,2-ETHANEDIOL × 3 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HSLO_THEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 13–302； UniProt 1–290 Author chain B； PDBConstruct 13–302； UniProt 1–290

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	1vq0
Deposition date deposition_date	2004-11-30
Structure title title	Crystal structure of 33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33) (TM1394) from Thermotoga maritima at 2.20 A resolution
Keywords keywords	;TM1394, 33 KDA chaperonin (heat shock protein 33 homolog) (HSP33), Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI, CHAPERONE ;; CHAPERONE
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.

1vq0__assembly_1__model_1

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

Download this curve (.dat)

1vq0__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1vq0__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	29.37 Å
Rg (electron density)	28.19 Å
Total Rg	29.02 Å
Atom count	4612
Residues	580
Excluded volume	82618 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1vq0__assembly_1__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 (6)

Entity 1 Entity 1 polymer

Description description	33 kDa chaperonin
Molecular weight formula_weight	34044.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	4889

MGSDKIHHHHHHMIYYGTMFDHKVRFSIVRMREVVEEARNRHALSYLATVVLGRALIGAALVTPWLAEKERWTLDIEGNGPIRRVVAQSTSEFTVRGYVANPKVELPLNEKGKFDVAGAIGQGVLRVVRDLGLKTPFVSQVPLVSGEIAEDLAYYFAVSEQIPSAFSIGVLVDSDGVKIAGGFAVQIIDRTLEQEKVEMIEKNIKNLPSISKLFQEAEPLDVLERIFGEKVGFVETAEIKYKCDCNREKAKNALLVLDKKELEDMRKEGKGEVVCKWCNTRYVFSEEELEELLKFKVDDSGS

Source Source

Source organism organism	Thermotoga maritima
NCBI taxonomy ID ncbi_taxonomy_id	2336
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	UNKNOWN LIGAND
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	273

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1vq0a1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.193 — Hsp33 domain
Superfamily Superfamily superfamily	d.193.1 — Hsp33 domain
Family Family family	d.193.1.1 — Hsp33 domain

Domain ID domain_id	d1vq0a2
Class class	g — Small proteins
Fold Fold fold	g.81 — HSP33 redox switch-like
Superfamily Superfamily superfamily	g.81.1 — HSP33 redox switch-like
Family Family family	g.81.1.1 — HSP33 redox switch-like

Domain ID domain_id	d1vq0a3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1vq0b1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.193 — Hsp33 domain
Superfamily Superfamily superfamily	d.193.1 — Hsp33 domain
Family Family family	d.193.1.1 — Hsp33 domain

Domain ID domain_id	d1vq0b2
Class class	g — Small proteins
Fold Fold fold	g.81 — HSP33 redox switch-like
Superfamily Superfamily superfamily	g.81.1 — HSP33 redox switch-like
Family Family family	g.81.1.1 — HSP33 redox switch-like

Domain ID domain_id	d1vq0b3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (4 domains)

Domain ID domain_id	1vq0A01
Class class	3 — Alpha Beta
Architecture architecture	55 — 3-Layer(bab) Sandwich
Topology topology	30 — Hsp33 domain
Homologous superfamily homologous superfamily	10 — Hsp33 domain

Domain ID domain_id	1vq0A02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1280 — CBS domain Like
Homologous superfamily homologous superfamily	10 — HSP33 redox switch-like

Domain ID domain_id	1vq0B01
Class class	3 — Alpha Beta
Architecture architecture	55 — 3-Layer(bab) Sandwich
Topology topology	30 — Hsp33 domain
Homologous superfamily homologous superfamily	10 — Hsp33 domain

Domain ID domain_id	1vq0B02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1280 — CBS domain Like
Homologous superfamily homologous superfamily	10 — HSP33 redox switch-like

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Unit-cell length a length_a	76.213 Å
Unit-cell length b length_b	101.673 Å
Unit-cell length c length_c	113.686 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	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	49.620 Å
R factor r_factor	0.2003
R_work r_work	0.1982
R_free r_free	0.2408

Crystal structure of 33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33) (TM1394) from Thermotoga maritima at 2.20 A resolution

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

33 kDa chaperonin

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

1vq0__assembly_1__model_1

1vq0__assembly_1__model_1 | I(q)

1vq0__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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Crystal structure of 33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33) (TM1394) from Thermotoga maritima at 2.20 A resolution

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

33 kDa chaperonin

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

1vq0__assembly_1__model_1

1vq0__assembly_1__model_1 | I(q)

1vq0__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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

CATH v4.4 (4 domains)

7. Citations (1)