1zt9

E. coli trp repressor, tetragonal crystal form

Method: X-RAY DIFFRACTION Dmax: 81.6 Å Quality: EXCELLENT

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

Trp operon repressor

Escherichia coli

UniProt P0A881

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 1–107 Chain B; UniProt 1–107 Not recorded SO4 SULFATE ION × 4 TRP TRYPTOPHAN × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;294 K;2.8 M ammonium sulfate plus 50 mM sodium, potassium phosphate buffer, 5 mM L-tryptophan, VAPOR DIFFUSION, HANGING DROP, temperature 294K, pH 5.60 Resolution 2.00 Å R-free 0.219
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–107 Chain E; UniProt 1–107 Not recorded SO4 SULFATE ION × 4 TRP TRYPTOPHAN × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;294 K;2.8 M ammonium sulfate plus 50 mM sodium, potassium phosphate buffer, 5 mM L-tryptophan, VAPOR DIFFUSION, HANGING DROP, temperature 294K, pH 5.60 Resolution 2.00 Å R-free 0.219
3 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–107 Chain B; UniProt 1–107 Chain D; UniProt 1–107 Chain E; UniProt 1–107 Not recorded SO4 SULFATE ION × 8 TRP TRYPTOPHAN × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;294 K;2.8 M ammonium sulfate plus 50 mM sodium, potassium phosphate buffer, 5 mM L-tryptophan, VAPOR DIFFUSION, HANGING DROP, temperature 294K, pH 5.60 Resolution 2.00 Å R-free 0.219
4 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–107 Chain B; UniProt 1–107 Chain D; UniProt 1–107 Chain E; UniProt 1–107 Not recorded SO4 SULFATE ION × 8 TRP TRYPTOPHAN × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;294 K;2.8 M ammonium sulfate plus 50 mM sodium, potassium phosphate buffer, 5 mM L-tryptophan, VAPOR DIFFUSION, HANGING DROP, temperature 294K, pH 5.60 Resolution 2.00 Å R-free 0.219
5 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–107 Chain B; UniProt 1–107 Chain D; UniProt 1–107 Chain E; UniProt 1–107 Not recorded SO4 SULFATE ION × 8 TRP TRYPTOPHAN × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;294 K;2.8 M ammonium sulfate plus 50 mM sodium, potassium phosphate buffer, 5 mM L-tryptophan, VAPOR DIFFUSION, HANGING DROP, temperature 294K, pH 5.60 Resolution 2.00 Å R-free 0.219

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.

26 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRPR_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–107; UniProt 1–107 Author chain B; PDBConstruct 1–107; UniProt 1–107 Author chain D; PDBConstruct 1–107; UniProt 1–107 Author chain E; PDBConstruct 1–107; UniProt 1–107

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 1zt9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1zt9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1zt9
Deposition date deposition_date2005-05-26
Structure title titleE. coli trp repressor, tetragonal crystal form
Keywords keywords;helix-turn-helix, DNA-binding protein, protein-protein interaction, L-tryptophan binding protein, bound sulfate anions, TRANSCRIPTION ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.54
Radius of gyration Rg (electron density) rg_electron24.27
Forward intensity I(0) i040399600.00
Molecular weight molecular_weight47770.0 kDa
Excluded volume excluded_volume59389 ų
Envelope volume envelope_volume74283 ų
Hydration-shell volume shell_volume25811 ų
Envelope diameter envelope_diameter84.3
Shell Rg shell_rg31.16
Envelope Rg envelope_rg24.25
Shape Rg shape_rg24.21
Total Rg total_rg25.25
Total atoms total_atoms3348
Residues n_residues404
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 dmax81.6
Rg (real space) rg_real25.48
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real4.0400e+07
I(0) uncertainty (real space) i0_real_error6.1080e+05
Rg (reciprocal space) rg_reciprocal25.50
I(0) (reciprocal space) i0_reciprocal40400000.0000
Solution quality estimate total_estimate0.9030
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.0
Skewness Skewness skewness0.257
Kurtosis Kurtosis kurtosis-0.437
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7171000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.980

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1zt9a_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.12 — TrpR-like
Family Family familya.4.12.1 — Trp repressor, TrpR
Domain ID domain_idd1zt9b_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.12 — TrpR-like
Family Family familya.4.12.1 — Trp repressor, TrpR
Domain ID domain_idd1zt9d_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.12 — TrpR-like
Family Family familya.4.12.1 — Trp repressor, TrpR
Domain ID domain_idd1zt9e_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.12 — TrpR-like
Family Family familya.4.12.1 — Trp repressor, TrpR

CATH v4.4 (4 domains)

Domain ID domain_id1zt9A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1270 — Trp Operon Repressor; Chain A
Homologous superfamily homologous superfamily10 — TrpR-like
Domain ID domain_id1zt9B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1270 — Trp Operon Repressor; Chain A
Homologous superfamily homologous superfamily10 — TrpR-like
Domain ID domain_id1zt9D00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1270 — Trp Operon Repressor; Chain A
Homologous superfamily homologous superfamily10 — TrpR-like
Domain ID domain_id1zt9E00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1270 — Trp Operon Repressor; Chain A
Homologous superfamily homologous superfamily10 — TrpR-like

8. Citations (2)

9. Files and Curves (10)