6e8e

Crystal structure of the Escherichia coli sliding clamp-MutL complex.

Method: X-RAY DIFFRACTION Dmax: 103.3 Å Quality: EXCELLENT

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

Beta sliding clamp,DNA mismatch repair protein MutL

Escherichia coli O139:H28 (strain E24377A / ETEC)

UniProt A7ZV39

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 466–569 Chain B; UniProt 466–569 Non-standard monomer:Yes (specific site not provided by mmCIF) GOL GLYCEROL × 6 SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;100 mM Bis-Tris pH 5.5, 2 M ammonium sulfate. Resolution 2.25 Å R-free 0.225

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name MUTL_ECO24
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 414–517; UniProt 466–569 Author chain B; PDBConstruct 414–517; UniProt 466–569

Beta sliding clamp,DNA mismatch repair protein MutL

Escherichia coli O139:H28 (strain E24377A / ETEC)

UniProt P0A988

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–366 Chain B; UniProt 1–366 Non-standard monomer:Yes (specific site not provided by mmCIF) GOL GLYCEROL × 6 SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;100 mM Bis-Tris pH 5.5, 2 M ammonium sulfate. Resolution 2.25 Å R-free 0.225

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.

53 other PDB entries and 60 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPO3B_ECOLI
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 39–404; UniProt 1–366 Author chain B; PDBConstruct 39–404; UniProt 1–366

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 6e8e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6e8e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6e8e
Deposition date deposition_date2018-07-28
Structure title titleCrystal structure of the Escherichia coli sliding clamp-MutL complex.
Keywords keywordsComplex, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.27
Radius of gyration Rg (electron density) rg_electron34.28
Forward intensity I(0) i0155429000.00
Molecular weight molecular_weight99844.0 kDa
Excluded volume excluded_volume125130 ų
Envelope volume envelope_volume173520 ų
Hydration-shell volume shell_volume41404 ų
Envelope diameter envelope_diameter107.6
Shell Rg shell_rg42.19
Envelope Rg envelope_rg32.81
Shape Rg shape_rg34.30
Total Rg total_rg34.84
Total atoms total_atoms7000
Residues n_residues922
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 dmax103.3
Rg (real space) rg_real35.07
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real1.5540e+08
I(0) uncertainty (real space) i0_real_error2.4980e+06
Rg (reciprocal space) rg_reciprocal35.20
I(0) (reciprocal space) i0_reciprocal155400000.0000
Solution quality estimate total_estimate0.9036
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.5
Skewness Skewness skewness-0.048
Kurtosis Kurtosis kurtosis-0.772
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46940000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.884

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)