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1azo

DNA MISMATCH REPAIR PROTEIN MUTH FROM E. COLI

Method: X-RAY DIFFRACTION Dmax: 63.0 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

MUTH

Escherichia coli

UniProt P06722

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–228 Non-standard monomer：Yes (specific site not provided by mmCIF) EDO 1,2-ETHANEDIOL × 11 X-RAY DIFFRACTION X-ray crystallization conditions：100 MM AMMONIUM ACETATE, 50 MM MAGNESIUM ACETATE, 1 MM DTT, 12-16 % PEG 6000 Resolution 1.70 Å R-free 0.263

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.

Other PDB Difference from Current Entry 1AZO Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2AZO DNA MISMATCH REPAIR PROTEIN MUTH FROM E. COLI Deposited 1997-11-20 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–228（228 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；100MM AMMONIUM ACETATE, 50 MM MAGNESIUM ACETATE, 1 MM DTT AND 12-16 % PEG6000, pH 6.0
Resolution 2.30 Å R-free 0.293
2AZO DNA MISMATCH REPAIR PROTEIN MUTH FROM E. COLI Deposited 1997-11-20 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–228（228 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；100MM AMMONIUM ACETATE, 50 MM MAGNESIUM ACETATE, 1 MM DTT AND 12-16 % PEG6000, pH 6.0
Resolution 2.30 Å R-free 0.293

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MUTH_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 5–232； UniProt 1–228

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 1azo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1azo
Deposition date deposition_date1997-11-19
Structure title titleDNA MISMATCH REPAIR PROTEIN MUTH FROM E. COLI
Keywords keywordsENDONUCLEASE, MUTH, DNA REPAIR, HYDROLASE; ENDONUCLEASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier19.83 Å
Radius of gyration Rg (electron density) rg_electron18.61 Å
Forward intensity I(0) i010614800.00
Molecular weight molecular_weight24784.0 kDa
Excluded volume excluded_volume31349 ų
Envelope volume envelope_volume37510 ų
Hydration-shell volume shell_volume17243 ų
Envelope diameter envelope_diameter64.7 Å
Shell Rg shell_rg24.31 Å
Envelope Rg envelope_rg18.74 Å
Shape Rg shape_rg18.57 Å
Total Rg total_rg19.63 Å
Total atoms total_atoms1740
Residues n_residues212
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax63.0 Å
Rg (real space) rg_real19.74 Å
Rg uncertainty (real space) rg_real_error0.35 Å
I(0) (real space) i0_real1.0610e+07
I(0) uncertainty (real space) i0_real_error1.3020e+05
Rg (reciprocal space) rg_reciprocal19.76 Å
I(0) (reciprocal space) i0_reciprocal10610000.0000
Solution quality estimate total_estimate0.9029
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.9 Å
Skewness Skewness skewness0.182
Kurtosis Kurtosis kurtosis-0.504
Angular range angular_range— – 0.4000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2790000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.997
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1azoa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.52 — Restriction endonuclease-like
Superfamily Superfamily superfamilyc.52.1 — Restriction endonuclease-like
Family Family familyc.52.1.14 — DNA mismatch repair protein MutH from

CATH v4.4 (1 domains)

Domain ID domain_id1azoA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology600 — ECO RV Endonuclease; Chain A
Homologous superfamily homologous superfamily10 — DNA mismatch repair MutH/Restriction endonuclease, type II
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8. Citations (1)

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9. Files and Curves (10)