2kek

Solution structure of a dimer of LAC repressor DNA-binding domain complexed to its natural operator O3

Method: SOLUTION NMR Dmax: 80.5 Å Quality: REASONABLE

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

Lactose operon repressor

Escherichia coli

UniProt P03023

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–DNA Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 1–62 Chain B; UniProt 1–62 Fragment:UNP residues 1-62 Mutation:V52C ;DNA (5'-D(*CP*GP*GP*CP*AP*GP*TP*GP*AP*GP*CP*GP*CP*AP*AP*CP*GP*CP*AP*AP*TP*TP*C)-3') ; × 1 ;DNA (5'-D(P*GP*AP*AP*TP*TP*GP*CP*GP*TP*TP*GP*CP*GP*CP*TP*CP*AP*CP*TP*GP*CP*CP*G)-3') ; × 1 SOLUTION NMR NMR measurement conditions:pH 6;315 K;Ionic strength (raw mmCIF value) 0.03;Pressure ambient NMR sample composition:0.7 mM DNA (5'-strand1-3'), 0.7 mM DNA (5'-strand2-3'), 0.7 mM Lac headpiece dimer, 5% D2O, 10 mM potassium phosphate, 20 mM potassium chloride, 5% U-100% 2H d8-glycerol, 0.01% sodium azide, 95% H2O/5% D2O | 95% H2O/5% D2O Resolution not provided

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.

21 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LACI_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–62; UniProt 1–62 Author chain B; PDBConstruct 1–62; UniProt 1–62

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 2kek

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2kek
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2kek
Deposition date deposition_date2009-01-30
Structure title titleSolution structure of a dimer of LAC repressor DNA-binding domain complexed to its natural operator O3
Keywords keywords;Lac repressor, lac operators, protein-DNA complex, DNA-binding, Repressor, Transcription, Transcription regulation, Transcription-DNA COMPLEX ;; Transcription/DNA
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier23.23
Radius of gyration Rg (electron density) rg_electron23.07
Forward intensity I(0) i02017920000.00
Molecular weight molecular_weight278130.0 kDa
Excluded volume excluded_volume306050 ų
Envelope volume envelope_volume65895 ų
Hydration-shell volume shell_volume23581 ų
Envelope diameter envelope_diameter91.5
Shell Rg shell_rg30.52
Envelope Rg envelope_rg24.93
Shape Rg shape_rg23.01
Total Rg total_rg23.32
Total atoms total_atoms33740
Residues n_residues1700
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 dmax80.5
Rg (real space) rg_real23.54
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real2.0180e+09
I(0) uncertainty (real space) i0_real_error2.7140e+07
Rg (reciprocal space) rg_reciprocal23.47
I(0) (reciprocal space) i0_reciprocal2018000000.0000
Solution quality estimate total_estimate0.7263
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.6
Skewness Skewness skewness0.583
Kurtosis Kurtosis kurtosis-0.307
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3040000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.651; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.486; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2keka_
Class classa — All alpha proteins
Fold Fold folda.35 — lambda repressor-like DNA-binding domains
Superfamily Superfamily superfamilya.35.1 — lambda repressor-like DNA-binding domains
Family Family familya.35.1.5 — GalR/LacI-like bacterial regulator
Domain ID domain_idd2kekb_
Class classa — All alpha proteins
Fold Fold folda.35 — lambda repressor-like DNA-binding domains
Superfamily Superfamily superfamilya.35.1 — lambda repressor-like DNA-binding domains
Family Family familya.35.1.5 — GalR/LacI-like bacterial regulator

CATH v4.4 (2 domains)

Domain ID domain_id2kekA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology260 — 434 Repressor (Amino-terminal Domain)
Homologous superfamily homologous superfamily40 — lambda repressor-like DNA-binding domains
Domain ID domain_id2kekB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology260 — 434 Repressor (Amino-terminal Domain)
Homologous superfamily homologous superfamily40 — lambda repressor-like DNA-binding domains

8. Citations (1)

9. Files and Curves (10)