1jyf

Structure of the Dimeric Lac Repressor with an 11-residue C-terminal Deletion.

Method: X-RAY DIFFRACTION Dmax: 71.1 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–349 Fragment:C-TERMINAL DELETION GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;295 K;Sodium Citrate, Sodium Acetate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 3.00 Å R-free 0.252

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 1–349; UniProt 1–349

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 1jyf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1jyf
Deposition date deposition_date2001-09-12
Structure title titleStructure of the Dimeric Lac Repressor with an 11-residue C-terminal Deletion.
Keywords keywordsGene Regulation, Protein Stability, Protein DNA-binding, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.08
Radius of gyration Rg (electron density) rg_electron19.22
Forward intensity I(0) i015078200.00
Molecular weight molecular_weight29113.0 kDa
Excluded volume excluded_volume36468 ų
Envelope volume envelope_volume41138 ų
Hydration-shell volume shell_volume18387 ų
Envelope diameter envelope_diameter69.9
Shell Rg shell_rg25.09
Envelope Rg envelope_rg19.46
Shape Rg shape_rg19.19
Total Rg total_rg20.13
Total atoms total_atoms2041
Residues n_residues272
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 dmax71.1
Rg (real space) rg_real20.09
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.5080e+07
I(0) uncertainty (real space) i0_real_error2.2880e+05
Rg (reciprocal space) rg_reciprocal20.09
I(0) (reciprocal space) i0_reciprocal15080000.0000
Solution quality estimate total_estimate0.5995
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.4
Skewness Skewness skewness0.416
Kurtosis Kurtosis kurtosis-0.254
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4862000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.684; Stabil: 1.000; Sysdev: 0.260; Positv: 1.000; Valcen: 0.959; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1jyfa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.93 — Periplasmic binding protein-like I
Superfamily Superfamily superfamilyc.93.1 — Periplasmic binding protein-like I
Family Family familyc.93.1.1 — L-arabinose binding protein-like

CATH v4.4 (2 domains)

Domain ID domain_id1jyfA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id1jyfA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator

8. Citations (1)

9. Files and Curves (10)