1tlv

Structure of the native and inactive LicT PRD from B. subtilis

Method: X-RAY DIFFRACTION

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

Transcription antiterminator licT

Bacillus subtilis

UniProt P39805

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name LICT_BACSU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–221; UniProt 57–274

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.

2. Structure Basics 2. Structure Basics

Entry ID entry_id1tlv
Deposition date deposition_date2004-06-10
Structure title titleStructure of the native and inactive LicT PRD from B. subtilis
Keywords keywords;transcriptional antitermination, conformational change, LicT, histidine phosphorylation, activation mechanism, HPr, dimer structure, phosphoenolpyruvate (PEP): sugar phosphotransferase system (PTS), PTS regulation domains (PRD), TRANSCRIPTION ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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.

1tlv__assembly_1__model_1

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

Download this curve (.dat)

1tlv__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1tlv__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)23.20 Å
Rg (electron density)22.20 Å
Total Rg23.14 Å
Atom count3416
Residues408
Excluded volume61742 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1tlv__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (2)

6. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1tlva1
Class classa — All alpha proteins
Fold Fold folda.142 — PTS-regulatory domain, PRD
Superfamily Superfamily superfamilya.142.1 — PTS-regulatory domain, PRD
Family Family familya.142.1.1 — PTS-regulatory domain, PRD
Domain ID domain_idd1tlva2
Class classa — All alpha proteins
Fold Fold folda.142 — PTS-regulatory domain, PRD
Superfamily Superfamily superfamilya.142.1 — PTS-regulatory domain, PRD
Family Family familya.142.1.1 — PTS-regulatory domain, PRD
Domain ID domain_idd1tlva3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id1tlvA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1790 — PTS-regulatory domain, PRD
Homologous superfamily homologous superfamily10 — PRD domain
Domain ID domain_id1tlvA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1790 — PTS-regulatory domain, PRD
Homologous superfamily homologous superfamily10 — PRD domain

7. Citations (2)