SAXSdb — 1tfe

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

ELONGATION FACTOR TS

Thermus thermophilus

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 55–196	Fragment：EF-TS DIMERIZATION DOMAIN, RESIDUES 55 - 196	No other associated polymer	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 1.70 Å R-free 0.285

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.

Other PDB	Difference from Current Entry 1TFE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AIP EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS Deposited 1997-04-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–196（196 aa） Chain D 1–196（196 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；60 MM CACODYLATE, PH 6.5 70 MM AMMONIUM SULFATE 8% PEG 8000	Resolution 3.00 Å R-free 0.289
1AIP EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS Deposited 1997-04-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain G 1–196（196 aa） Chain H 1–196（196 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；60 MM CACODYLATE, PH 6.5 70 MM AMMONIUM SULFATE 8% PEG 8000	Resolution 3.00 Å R-free 0.289

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	EFTS_THET8
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–142； UniProt 55–196

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	1tfe
Deposition date deposition_date	1996-04-16
Structure title title	DIMERIZATION DOMAIN OF EF-TS FROM T. THERMOPHILUS
Keywords keywords	ELONGATION FACTOR; ELONGATION FACTOR
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	18.88 Å
Radius of gyration Rg (electron density) rg_electron	18.09 Å
Forward intensity I(0) i0	4958200.00
Molecular weight molecular_weight	16319.0 kDa
Excluded volume excluded_volume	20579 Å³
Envelope volume envelope_volume	24629 Å³
Hydration-shell volume shell_volume	12657 Å³
Envelope diameter envelope_diameter	65.9 Å
Shell Rg shell_rg	22.45 Å
Envelope Rg envelope_rg	18.46 Å
Shape Rg shape_rg	18.08 Å
Total Rg total_rg	18.88 Å
Total atoms total_atoms	1148
Residues n_residues	142
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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

Maximum dimension Dmax dmax	67.8 Å
Rg (real space) rg_real	19.00 Å
Rg uncertainty (real space) rg_real_error	0.57 Å
I(0) (real space) i0_real	4.9580e+06
I(0) uncertainty (real space) i0_real_error	6.7400e+04
Rg (reciprocal space) rg_reciprocal	18.98 Å
I(0) (reciprocal space) i0_reciprocal	4958000.0000
Solution quality estimate total_estimate	0.8449
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.8 Å
Skewness Skewness skewness	0.482
Kurtosis Kurtosis kurtosis	-0.190
Angular range angular_range	— – 0.4200 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	687600.0000
Real-space data points n_real_points	73
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.755; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.737; Smooth: 0.979

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1tfea_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.43 — EF-Ts domain-like
Superfamily Superfamily superfamily	d.43.1 — Elongation factor Ts (EF-Ts), dimerisation domain
Family Family family	d.43.1.1 — Elongation factor Ts (EF-Ts), dimerisation domain

CATH v4.4 (2 domains)

Domain ID domain_id	1tfeA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	479 — Tetrahydropterin Synthase; Chain A
Homologous superfamily homologous superfamily	20 — Elongation factor Ts, dimerisation domain

Domain ID domain_id	1tfeA02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	20 —

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8. Citations (1)

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Unit-cell length a length_a	60.100 Å
Unit-cell length b length_b	60.100 Å
Unit-cell length c length_c	94.300 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 31 2 1
Space-group number int_tables_number	152
Crystal system crystal_system	—

Resolution resolution	1.700 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.2070
R_work r_work	0.2070
R_free r_free	0.2850

Description description	ELONGATION FACTOR TS
Molecular weight formula_weight	16728.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1935

DIMERIZATION DOMAIN OF EF-TS FROM T. THERMOPHILUS

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

ELONGATION FACTOR TS

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Thermus thermophilus
NCBI Class编号 ncbi_taxonomy_id	274
宿主生物 host_organism	Escherichia coli BL21(DE3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	259

fit	/app/data/saxs_computation/tf/1tfe/1tfe.fit
pddf	/app/data/pr_computation/tf/1tfe/1tfe.pr.out
profile	/app/data/saxs_computation/tf/1tfe/1tfe.dat