7ou4

The structure of MutS bound to one molecule of ATP and one molecule of ADP

Method: ELECTRON MICROSCOPY Dmax: 108.5 Å Quality: GOOD

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

DNA mismatch repair protein MutS

Escherichia coli

UniProt P23909

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 1–800 Chain B; UniProt 1–800 Not recorded MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 Å

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.

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

View Construct and Data Evidence
UniProt name MUTS_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–806; UniProt 1–800 Author chain B; PDBConstruct 7–806; UniProt 1–800

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 7ou4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ou4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ou4
Deposition date deposition_date2021-06-11
Structure title titleThe structure of MutS bound to one molecule of ATP and one molecule of ADP
Keywords keywordsDNA mismatch repair protein, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.98
Radius of gyration Rg (electron density) rg_electron34.25
Forward intensity I(0) i0382031000.00
Molecular weight molecular_weight156070.0 kDa
Excluded volume excluded_volume195100 ų
Envelope volume envelope_volume257330 ų
Hydration-shell volume shell_volume59779 ų
Envelope diameter envelope_diameter113.7
Shell Rg shell_rg43.09
Envelope Rg envelope_rg33.62
Shape Rg shape_rg34.26
Total Rg total_rg34.84
Total atoms total_atoms10954
Residues n_residues1389
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 dmax108.5
Rg (real space) rg_real34.76
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real3.8200e+08
I(0) uncertainty (real space) i0_real_error6.6900e+06
Rg (reciprocal space) rg_reciprocal34.90
I(0) (reciprocal space) i0_reciprocal382100000.0000
Solution quality estimate total_estimate0.8946
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.8
Skewness Skewness skewness0.108
Kurtosis Kurtosis kurtosis-0.472
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha79000000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.908; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.930

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7ou4A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1170 — MutS, DNA mismatch repair protein, domain I
Homologous superfamily homologous superfamily10 — DNA repair protein MutS, domain I
Domain ID domain_id7ou4A02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily110 — MutS, connector domain
Domain ID domain_id7ou4B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1170 — MutS, DNA mismatch repair protein, domain I
Homologous superfamily homologous superfamily10 — DNA repair protein MutS, domain I

8. Citations (1)

9. Files and Curves (10)