1xb2

Crystal Structure of Bos taurus mitochondrial Elongation Factor Tu/Ts Complex

Method: X-RAY DIFFRACTION

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

Elongation factor Tu, mitochondrial

Bos taurus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Elongation factor Ts, mitochondrial × 1 （P43896） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	EFTU_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–409； UniProt 44–452

Elongation factor Ts, mitochondrial

Bos taurus

UniProt P43896

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Elongation factor Tu, mitochondrial × 1 （P49410） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	EFTS_BOVIN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–283； UniProt 56–338

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	1xb2
Deposition date deposition_date	2004-08-27
Structure title title	Crystal Structure of Bos taurus mitochondrial Elongation Factor Tu/Ts Complex
Keywords keywords	Protein-protein complex, TRANSLATION; TRANSLATION
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.

1xb2__assembly_1__model_1

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

Download this curve (.dat)

1xb2__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1xb2__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	30.20 Å
Rg (electron density)	29.55 Å
Total Rg	30.17 Å
Atom count	4964
Residues	634
Excluded volume	88965 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1xb2__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 (3)

Entity 1 Entity 1 polymer

Description description	Elongation factor Tu, mitochondrial
Molecular weight formula_weight	45658.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	5294

AVEAKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPIIVGSALCALEQRDPELGLKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECEFLGHSKNIRTVVTGIEMFHKSLDRAEAGDNLGALVRGLKREDLRRGLVMAKPGSIQPHQKVEAQVYILTKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPGKELAMPGEDLKLTLILRQPMILEKGQRFTLRDGNRTIGTGLVTDTPAMTEEDKNIKWS

Source Source

Source organism organism	Bos taurus
Common name common_name	cattle
NCBI taxonomy ID ncbi_taxonomy_id	9913
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Elongation factor Ts, mitochondrial
Molecular weight formula_weight	31849.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

SASSKELLMKLRRKTGYSFINCKKALETCGGDLKQAESWLHKQAQKEGWSKAARLHGRKTKEGLIGLLQEGDTTVLVEVNCETDFVSRNLKFQQLVQQVALGTLLHCQNLKDQLSTYSKGFLNSSELSELPAGPEREGSLKDQLALAIGKLGENMILKRAAWVKVPAGFYVGSYVHGAMHSPSLHNLVLGKYGALVICETSELKANLADLGRRLGQHVVGMAPLSVGSLDDEPGGEAETKMLSQPYLLDPSITLGQYVQPHGVSVVDFVRFECGEGEDAADAELEHHHHHH

Source Source

Source organism organism	Bos taurus
Common name common_name	cattle
NCBI taxonomy ID ncbi_taxonomy_id	9913
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	322

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1xb2a1
Class class	b — All beta proteins
Fold Fold fold	b.43 — Reductase/isomerase/elongation factor common domain
Superfamily Superfamily superfamily	b.43.3 — Translation proteins
Family Family family	b.43.3.1 — Elongation factors

Domain ID domain_id	d1xb2a2
Class class	b — All beta proteins
Fold Fold fold	b.44 — Elongation factor/aminomethyltransferase common domain
Superfamily Superfamily superfamily	b.44.1 — EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
Family Family family	b.44.1.1 — EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain

Domain ID domain_id	d1xb2a3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.8 — G proteins

Domain ID domain_id	d1xb2b1
Class class	a — All alpha proteins
Fold Fold fold	a.5 — RuvA C-terminal domain-like
Superfamily Superfamily superfamily	a.5.2 — UBA-like
Family Family family	a.5.2.2 — TS-N domain

Domain ID domain_id	d1xb2b2
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

Domain ID domain_id	d1xb2b3
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 (6 domains)

Domain ID domain_id	1xb2A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	1xb2A02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	10 — Translation factors

Domain ID domain_id	1xb2A03
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	10 — Translation factors

Domain ID domain_id	1xb2B01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily	10 — Ubiquitin-associated (UBA) domain

Domain ID domain_id	1xb2B02
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	1xb2B03
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

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Unit-cell length a length_a	94.000 Å
Unit-cell length b length_b	149.300 Å
Unit-cell length c length_c	70.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	125.20 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2190
R_work r_work	0.2180
R_free r_free	0.2470

Crystal Structure of Bos taurus mitochondrial Elongation Factor Tu/Ts Complex

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

Elongation factor Tu, mitochondrial

State in the Current Structure

Other States of the Same Protein in the Database

Elongation factor Ts, mitochondrial

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

1xb2__assembly_1__model_1

1xb2__assembly_1__model_1 | I(q)

1xb2__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (1)

Crystal Structure of Bos taurus mitochondrial Elongation Factor Tu/Ts Complex

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

Elongation factor Tu, mitochondrial

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Elongation factor Ts, mitochondrial

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

1xb2__assembly_1__model_1

1xb2__assembly_1__model_1 | I(q)

1xb2__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (1)