SAXSdb — 3gty

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

Trigger factor

Thermotoga maritima

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	30S ribosomal protein S7 × 1 （P38526）	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TIG_THEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain X； PDBConstruct 1–425； UniProt 1–425

30S ribosomal protein S7

Thermotoga maritima

UniProt P38526

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Trigger factor × 1 （Q9WZF8）	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RS7_THEMA
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain S； PDBConstruct 3–149； UniProt 9–155

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	3gty
Deposition date deposition_date	2009-03-28
Structure title title	Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone
Keywords keywords	;Chaperone-Client Complex, Cell cycle, Cell division, Chaperone, Isomerase, Rotamase, Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding, tRNA-binding, Chaperone-Ribosomal protein COMPLEX ;; Chaperone/Ribosomal 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.

3gty__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3gty__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3gty__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	35.85 Å
Rg (electron density)	35.84 Å
Total Rg	36.06 Å
Atom count	3405
Residues	412
Excluded volume	60970 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3gty__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3gty__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3gty__assembly_3__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)

Entity 1 Entity 1 polymer

Description description	Trigger factor
Molecular weight formula_weight	51048.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	X
Atom count atom_count	4610

MEVKELERDKNRVVLEYVFGAEEIAQAEDKAVRYLNQRVEIPGFRKGRIPKNVLKMKLGEEFQEYTLDFLMDLIPDTLKDRKLILSPIVTERELKDVTARVVVEVHEEPEVRIGDISKIEVEKVDEEKVLEKYVERRIEDLRESHALLEPKEGPAEAGDLVRVNMEVYNEEGKKLTSREYEYVISEDEDRPFVKDLVGKKKGDVVEIEREYEGKKYTYKLEVEEVYKRTLPEIGDELAKSVNNEFETLEQLKESLKKEGKEIYDVEMKESMREQLLEKLPEIVEIEISDRTLEILVNEAINRLKREGRYEQIVSSYESEEKFREELKERILDDIKRDRVIEVLAQEKGISVNDEELEKEAEELAPFWGISPDRAKSLVKARQDLREELRWAILKRKVLDLLLQEVKVKVVEPKGEGDDSEGKEDNLEHHHHHH

Source Source

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

Entity 2 Entity 2 polymer

Description description	30S ribosomal protein S7
Molecular weight formula_weight	17124.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	S

MGRQIPPDPVFGDVLVAKLINRVMWDGKKTIAQKIVYGAFDIIREKTKKDPLEVFRQAVENVKPVLEVRPRRVGGATYQVPIEVQEPRRTSLALRWIVEAARAKKGRPMKEKLAEEIIAAYNNTGTAIKKKEDTHRMAEANRAFAHYRW

Source Source

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

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	3gtyS00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	455 — Ribosomal Protein S7
Homologous superfamily homologous superfamily	10 — Ribosomal protein S7/S5

Domain ID domain_id	3gtyX01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	1050 — Trigger factor ribosome-binding domain

Domain ID domain_id	3gtyX02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily	30 — Transcription elongation factor, GreA/GreB, C-terminal domain

Domain ID domain_id	3gtyX03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3120 — Trigger factor, domain 2
Homologous superfamily homologous superfamily	10 — Trigger factor, C-terminal domain

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Unit-cell length a length_a	94.162 Å
Unit-cell length b length_b	94.162 Å
Unit-cell length c length_c	193.072 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 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	—

Resolution resolution	3.400 Å
Low-resolution limit resolution_low	12.000 Å
R factor r_factor	0.2610
R_work r_work	0.2570
R_free r_free	0.3290

Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone

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

Trigger factor

State in the Current Structure

Other States of the Same Protein in the Database

30S ribosomal protein S7

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

3gty__assembly_2__model_1

3gty__assembly_2__model_1 | I(q)

3gty__assembly_2__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) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)

Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone

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

Trigger factor

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

30S ribosomal protein S7

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

3gty__assembly_2__model_1

3gty__assembly_2__model_1 | I(q)

3gty__assembly_2__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) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)