SAXSdb — 2azo

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

MUTH

Escherichia coli

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	Not recorded	No other associated polymer	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
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 1–228	Not recorded	No other associated polymer	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

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 2AZO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AZO DNA MISMATCH REPAIR PROTEIN MUTH FROM E. COLI Deposited 1997-11-19	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）	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

1 other PDB entries and 1 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 Author chain B； 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2azo
Deposition date deposition_date	1997-11-20
Structure title title	DNA MISMATCH REPAIR PROTEIN MUTH FROM E. COLI
Keywords keywords	ENDONUCLEASE, MUTH, DNA REPAIR, HYDROLASE; ENDONUCLEASE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	27.52 Å
Radius of gyration Rg (electron density) rg_electron	26.70 Å
Forward intensity I(0) i0	39008100.00
Molecular weight molecular_weight	49677.0 kDa
Excluded volume excluded_volume	62922 Å³
Envelope volume envelope_volume	80340 Å³
Hydration-shell volume shell_volume	26174 Å³
Envelope diameter envelope_diameter	99.5 Å
Shell Rg shell_rg	32.39 Å
Envelope Rg envelope_rg	26.89 Å
Shape Rg shape_rg	26.65 Å
Total Rg total_rg	27.49 Å
Total atoms total_atoms	3508
Residues n_residues	445
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	95.7 Å
Rg (real space) rg_real	27.63 Å
Rg uncertainty (real space) rg_real_error	0.91 Å
I(0) (real space) i0_real	3.9010e+07
I(0) uncertainty (real space) i0_real_error	7.0270e+05
Rg (reciprocal space) rg_reciprocal	27.60 Å
I(0) (reciprocal space) i0_reciprocal	39010000.0000
Solution quality estimate total_estimate	0.8666
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	33.0 Å
Skewness Skewness skewness	0.460
Kurtosis Kurtosis kurtosis	-0.134
Angular range angular_range	— – 0.2900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	8263000.0000
Real-space data points n_real_points	59
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.804; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.942; Smooth: 0.908

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2azoa_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.52 — Restriction endonuclease-like
Superfamily Superfamily superfamily	c.52.1 — Restriction endonuclease-like
Family Family family	c.52.1.14 — DNA mismatch repair protein MutH from

Domain ID domain_id	d2azob_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.52 — Restriction endonuclease-like
Superfamily Superfamily superfamily	c.52.1 — Restriction endonuclease-like
Family Family family	c.52.1.14 — DNA mismatch repair protein MutH from

CATH v4.4 (2 domains)

Domain ID domain_id	2azoA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	600 — ECO RV Endonuclease; Chain A
Homologous superfamily homologous superfamily	10 — DNA mismatch repair MutH/Restriction endonuclease, type II

Domain ID domain_id	2azoB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	600 — ECO RV Endonuclease; Chain A
Homologous superfamily homologous superfamily	10 — DNA mismatch repair MutH/Restriction endonuclease, type II

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8. Citations (1)

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Unit-cell length a length_a	39.860 Å
Unit-cell length b length_b	111.570 Å
Unit-cell length c length_c	54.930 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	96.53 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2020
R_work r_work	0.2020
R_free r_free	0.2930

Description description	MUTH
Molecular weight formula_weight	25840.7 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3652

DNA MISMATCH REPAIR PROTEIN MUTH FROM E. COLI

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

MUTH

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	83333
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	144

fit	/app/data/saxs_computation/az/2azo/2azo.fit
pddf	/app/data/pr_computation/az/2azo/2azo.pr.out
profile	/app/data/saxs_computation/az/2azo/2azo.dat