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1dg1

WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ELONGATION FACTOR TU

OrganismNot specified

UniProt P0A6N1

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 MAGNESIUM ION × 2 GUANOSINE-5'-DIPHOSPHATE × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1efc 1efc 1etu 1qzd 2bvn 2bvn

6 assemblies

Homodimer
1dg1 2hcj 2hdn 2hdn 2hdn 2hdn 2hdn 2hdn

8 assemblies

Homotetramer
2hdn 2hdn 2hdn

3 assemblies

Other homooligomers

None

Heteromeric or nucleic-acid complex
1d8t 1d8t 1efu 1ls2 3ep2 3eq3 3eq4 4v69

8 assemblies

View Construct and Data Evidence
UniProt name EFTU_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain G； PDBConstruct 1–394； UniProt 1–394 Author chain H； PDBConstruct 1–394； UniProt 1–394

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_id1dg1
Deposition date deposition_date1999-11-22
Structure title titleWHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).
Keywords keywordsELONGATION FACTOR, TRNA BINDING, ALPHA BETA SHIFT, TS BINDING PROTEIN, GTPASE, GDP BINDING, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodX-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.

1dg1__assembly_1__model_1

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

Download this curve (.dat)

1dg1__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1dg1__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）34.69 Å
Rg (electron density)34.21 Å
Total Rg34.85 Å
Atom count5984
Residues770
Excluded volume106520 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1dg1__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 (4)

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1dg1g1
Class classb — All beta proteins
Fold Fold foldb.43 — Reductase/isomerase/elongation factor common domain
Superfamily Superfamily superfamilyb.43.3 — Translation proteins
Family Family familyb.43.3.1 — Elongation factors
Domain ID domain_idd1dg1g2
Class classb — All beta proteins
Fold Fold foldb.44 — Elongation factor/aminomethyltransferase common domain
Superfamily Superfamily superfamilyb.44.1 — EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
Family Family familyb.44.1.1 — EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
Domain ID domain_idd1dg1g3
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd1dg1h1
Class classb — All beta proteins
Fold Fold foldb.43 — Reductase/isomerase/elongation factor common domain
Superfamily Superfamily superfamilyb.43.3 — Translation proteins
Family Family familyb.43.3.1 — Elongation factors
Domain ID domain_idd1dg1h2
Class classb — All beta proteins
Fold Fold foldb.44 — Elongation factor/aminomethyltransferase common domain
Superfamily Superfamily superfamilyb.44.1 — EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
Family Family familyb.44.1.1 — EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
Domain ID domain_idd1dg1h3
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins

CATH v4.4 (6 domains)

Domain ID domain_id1dg1G01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id1dg1G02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily10 — Translation factors
Domain ID domain_id1dg1G03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily10 — Translation factors
Domain ID domain_id1dg1H01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id1dg1H02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily10 — Translation factors
Domain ID domain_id1dg1H03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily10 — Translation factors
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7. Citations (1)