1a6i

TET REPRESSOR, CLASS D VARIANT

Method: X-RAY DIFFRACTION Dmax: 73.3 Å Quality: GOOD

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

TETRACYCLINE REPRESSOR PROTEIN CLASS D

Escherichia coli

UniProt P0ACT4

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 2–217 Mutation:A2S, N5D, R6K, E7S, S8K, D11N, A12S, T20V, D23E, I36V No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 2.40 Å R-free 0.275

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.

45 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TETR4_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–217; UniProt 2–217

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1a6i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a6i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a6i
Deposition date deposition_date1998-02-25
Structure title titleTET REPRESSOR, CLASS D VARIANT
Keywords keywordsTRANSCRIPTION REGULATION, REPRESSOR, DNA-BINDING; TRANSCRIPTION REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.85
Radius of gyration Rg (electron density) rg_electron20.38
Forward intensity I(0) i08734870.00
Molecular weight molecular_weight21801.0 kDa
Excluded volume excluded_volume27387 ų
Envelope volume envelope_volume34725 ų
Hydration-shell volume shell_volume15572 ų
Envelope diameter envelope_diameter75.1
Shell Rg shell_rg25.33
Envelope Rg envelope_rg20.85
Shape Rg shape_rg20.35
Total Rg total_rg21.27
Total atoms total_atoms1539
Residues n_residues193
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax73.3
Rg (real space) rg_real20.94
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real8.7350e+06
I(0) uncertainty (real space) i0_real_error1.3130e+05
Rg (reciprocal space) rg_reciprocal20.92
I(0) (reciprocal space) i0_reciprocal8735000.0000
Solution quality estimate total_estimate0.7697
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.2
Skewness Skewness skewness0.439
Kurtosis Kurtosis kurtosis-0.287
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1956000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.724; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.829; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1a6ia1
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.1 — Homeodomain-like
Family Family familya.4.1.9 — Tetracyclin repressor-like, N-terminal domain
Domain ID domain_idd1a6ia2
Class classa — All alpha proteins
Fold Fold folda.121 — Tetracyclin repressor-like, C-terminal domain
Superfamily Superfamily superfamilya.121.1 — Tetracyclin repressor-like, C-terminal domain
Family Family familya.121.1.1 — Tetracyclin repressor-like, C-terminal domain

CATH v4.4 (2 domains)

Domain ID domain_id1a6iA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily60 — Homeodomain-like
Domain ID domain_id1a6iA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology357 — Tetracycline Repressor; domain 2
Homologous superfamily homologous superfamily10 — Tetracycline Repressor, domain 2

8. Citations (3)

9. Files and Curves (10)