2mn6

Solution structure of dimeric TatA of twin-arginine translocation system from E. coli

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Sec-independent protein translocase protein TatA

Escherichia coli

UniProt P69428

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name TATA_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–92; UniProt 1–89 Author chain B; PDBConstruct 4–92; UniProt 1–89

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_id2mn6
Deposition date deposition_date2014-03-31
Structure title titleSolution structure of dimeric TatA of twin-arginine translocation system from E. coli
Keywords keywordsTRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodSOLUTION NMR
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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.

2mn6__assembly_1__model_2

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

Download this curve (.dat)

2mn6__assembly_1__model_2 | I(q)

10-2 10-1 105 106 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

2mn6__assembly_1__model_2 | 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)16.65 Å
Rg (electron density)15.18 Å
Total Rg16.44 Å
Atom count1438
Residues94
Excluded volume12794 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2mn6__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 2mn6__assembly_1__model_2 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 2mn6__assembly_1__model_3 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 2mn6__assembly_1__model_4 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 2mn6__assembly_1__model_5 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 2mn6__assembly_1__model_6 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 2mn6__assembly_1__model_7 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 2mn6__assembly_1__model_8 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 2mn6__assembly_1__model_9 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 2mn6__assembly_1__model_10 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 (1)

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6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id2mn6A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily3310 —
Domain ID domain_id2mn6B00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily3310 —
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7. Citations (1)