3gu0

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

Method: X-RAY DIFFRACTION Dmax: 115.7 Å Quality: GOOD

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

Trigger factor

Thermotoga maritima

UniProt Q9WZF8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–405 Fragment:residues 1-405 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;10-15% PEG4000, 200 MgCl2, 100 Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.50 Å R-free 0.358

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TIG_THEMA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–405; UniProt 1–405

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.

SAXS scattering curve SAXS Profile

SAXS profile for 3gu0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3gu0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3gu0
Deposition date deposition_date2009-03-28
Structure title titlePromiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone
Keywords keywordsmolecular chaperone, Cell cycle, Cell division, Chaperone, Isomerase, Rotamase; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier35.33
Radius of gyration Rg (electron density) rg_electron35.34
Forward intensity I(0) i036584900.00
Molecular weight molecular_weight47838.0 kDa
Excluded volume excluded_volume60213 ų
Envelope volume envelope_volume100700 ų
Hydration-shell volume shell_volume26890 ų
Envelope diameter envelope_diameter116.8
Shell Rg shell_rg37.49
Envelope Rg envelope_rg33.71
Shape Rg shape_rg35.33
Total Rg total_rg35.58
Total atoms total_atoms3368
Residues n_residues406
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax115.7
Rg (real space) rg_real35.57
Rg uncertainty (real space) rg_real_error1.47
I(0) (real space) i0_real3.6580e+07
I(0) uncertainty (real space) i0_real_error7.0410e+05
Rg (reciprocal space) rg_reciprocal35.42
I(0) (reciprocal space) i0_reciprocal36580000.0000
Solution quality estimate total_estimate0.8409
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.1
Skewness Skewness skewness0.410
Kurtosis Kurtosis kurtosis-0.454
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1569000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.846; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.853; Smooth: 0.537

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id3gu0A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily1050 — Trigger factor ribosome-binding domain
Domain ID domain_id3gu0A02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily30 — Transcription elongation factor, GreA/GreB, C-terminal domain
Domain ID domain_id3gu0A03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology3120 — Trigger factor, domain 2
Homologous superfamily homologous superfamily10 — Trigger factor, C-terminal domain

8. Citations (1)

9. Files and Curves (10)