SAXSdb — 1f43

▼

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

MATING-TYPE PROTEIN A-1

Saccharomyces cerevisiae

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 66–126	Fragment：HOMEODOMAIN, C-TERMINAL DOMAIN (66-126)	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 4.5；298 K；Ionic strength (raw mmCIF value) 100 mM KCl；Pressure ambient NMR measurement conditions：pH 4.5；298 K；Ionic strength (raw mmCIF value) 100 mM KCl；Pressure ambient NMR measurement conditions：pH 4.5；298 K；Ionic strength (raw mmCIF value) 100 mM KCl；Pressure ambient NMR sample composition：1.5 mM MATa1(66-126) U-15N,13C 25 mM deuterated acetate, pH 4.5, 100 mM KCl, 0.01% NaN3; 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition：1.5 mM MATa1 (66-126) U-15N 25 mM deuterated acetate, pH 4.5, 100 mM KCl, 0.01% NaN3; 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition：1.5 mM MATa1 (66-126) 25 mM deuterated acetate, pH 4.5, 100 mM KCl, 0.01% NaN3; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided

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 1F43	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AKH MAT A1/ALPHA2/DNA TERNARY COMPLEX Deposited 1997-05-19	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 2 PDB declaration: tetrameric	Chain A 66–126（61 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；100MM HEPES PH 7.0, 20MM CACL2, 5MM [CO(NH3)6]CL3., VAPOR DIFFUSION, HANGING DROP, temperature 295.00K	Resolution 2.50 Å R-free 0.302
1LE8 Crystal Structure of the MATa1/MATalpha2-3A Heterodimer Bound to DNA Complex Deposited 2002-04-09	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 2 PDB declaration: tetrameric	Chain A 74–126（53 aa） Fragment：residues 74-126	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；10% PEG400, 8 mM Co(NH3)6Cl3, 10 mM CaCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.30 Å R-free 0.299
1MH3 maltose binding-a1 homeodomain protein chimera, crystal form I Deposited 2002-08-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 77–126（50 aa）	Mutation：E359A, K362A, D363A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；amonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.10 Å R-free 0.262
1MH4 maltose binding-a1 homeodomain protein chimera, crystal form II Deposited 2002-08-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 77–126（50 aa）	Mutation：E359A, K362A, D363A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；PEG 6000, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.30 Å R-free 0.293
1YRN CRYSTAL STRUCTURE OF THE MATA1/MATALPHA2 HOMEODOMAIN HETERODIMER BOUND TO DNA Deposited 1995-11-02	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 2 PDB declaration: tetrameric	Chain A 66–126（61 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.298

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MATA1_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–61； UniProt 66–126

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1f43
Deposition date deposition_date	2000-06-07
Structure title title	SOLUTION STRUCTURE OF THE MATA1 HOMEODOMAIN
Keywords keywords	Homeodomain, helix-turn-helix, TRANSCRIPTION; TRANSCRIPTION
Experimental Method method	SOLUTION NMR

▼

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

Radius of gyration Rg (Guinier) rg_guinier	12.35 Å
Radius of gyration Rg (electron density) rg_electron	12.15 Å
Forward intensity I(0) i0	281282000.00
Molecular weight molecular_weight	143190.0 kDa
Excluded volume excluded_volume	181490 Å³
Envelope volume envelope_volume	31608 Å³
Hydration-shell volume shell_volume	15775 Å³
Envelope diameter envelope_diameter	53.5 Å
Shell Rg shell_rg	22.95 Å
Envelope Rg envelope_rg	17.47 Å
Shape Rg shape_rg	12.06 Å
Total Rg total_rg	12.85 Å
Total atoms total_atoms	20980
Residues n_residues	1220
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

▼

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

Maximum dimension Dmax dmax	48.0 Å
Rg (real space) rg_real	12.36 Å
Rg uncertainty (real space) rg_real_error	0.48 Å
I(0) (real space) i0_real	2.8130e+08
I(0) uncertainty (real space) i0_real_error	3.2700e+06
Rg (reciprocal space) rg_reciprocal	12.36 Å
I(0) (reciprocal space) i0_reciprocal	281300000.0000
Solution quality estimate total_estimate	0.6669
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	14.6 Å
Skewness Skewness skewness	0.374
Kurtosis Kurtosis kurtosis	0.086
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	123200.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.267; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.868; Smooth: 0.000

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1f43a_
Class class	a — All alpha proteins
Fold Fold fold	a.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamily	a.4.1 — Homeodomain-like
Family Family family	a.4.1.1 — Homeodomain

CATH v4.4 (1 domains)

Domain ID domain_id	1f43A00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	60 — Homeodomain-like

▶

8. Citations (1)

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

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

Description description	MATING-TYPE PROTEIN A-1
Molecular weight formula_weight	7164.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	20980

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932
宿主生物 host_organism	Escherichia coli

SOLUTION STRUCTURE OF THE MATA1 HOMEODOMAIN

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

MATING-TYPE PROTEIN A-1

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/f4/1f43/1f43.fit
pddf	/app/data/pr_computation/f4/1f43/1f43.pr.out
profile	/app/data/saxs_computation/f4/1f43/1f43.dat