SAXSdb — 4pl9

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

Ethylene receptor 1

Arabidopsis thaliana

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 407–589	Fragment：residue 407-589	CD CADMIUM ION × 11 CL CHLORIDE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；292 K；50 mM Cadmimum sulfate, 0.1 M HEPES pH 7.5, 1.0M Sodium acetate	Resolution 1.90 Å R-free 0.182

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 4PL9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1DCF CRYSTAL STRUCTURE OF THE RECEIVER DOMAIN OF THE ETHYLENE RECEPTOR OF ARABIDOPSIS THALIANA Deposited 1999-11-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 603–738（136 aa） Fragment：RECEIVER DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；277 K；Li2SO4, HEPES, pH 7.4, VAPOR DIFFUSION, HANGING DROP	Resolution 2.50 Å R-free 0.271

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

View Construct and Data Evidence

UniProt name	ETR1_ARATH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–183； UniProt 407–589

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	4pl9
Deposition date deposition_date	2014-05-16
Structure title title	Structure of the catalytic domain of ETR1 from Arabidopsis thaliana
Keywords keywords	ETR1, Histidine Kinase, ethylene receptor, Cadmium, ADP, transferase; TRANSFERASE
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	16.43 Å
Radius of gyration Rg (electron density) rg_electron	15.18 Å
Forward intensity I(0) i0	4960860.00
Molecular weight molecular_weight	16889.0 kDa
Excluded volume excluded_volume	21609 Å³
Envelope volume envelope_volume	24389 Å³
Hydration-shell volume shell_volume	13632 Å³
Envelope diameter envelope_diameter	50.8 Å
Shell Rg shell_rg	21.00 Å
Envelope Rg envelope_rg	15.56 Å
Shape Rg shape_rg	15.17 Å
Total Rg total_rg	16.36 Å
Total atoms total_atoms	2433
Residues n_residues	150
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	51.8 Å
Rg (real space) rg_real	16.33 Å
Rg uncertainty (real space) rg_real_error	0.23 Å
I(0) (real space) i0_real	4.9610e+06
I(0) uncertainty (real space) i0_real_error	5.2480e+04
Rg (reciprocal space) rg_reciprocal	16.34 Å
I(0) (reciprocal space) i0_reciprocal	4961000.0000
Solution quality estimate total_estimate	0.8991
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.9 Å
Skewness Skewness skewness	0.165
Kurtosis Kurtosis kurtosis	-0.414
Angular range angular_range	— – 0.4850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	687300.0000
Real-space data points n_real_points	79
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.982

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Ethylene receptor 1
Molecular weight formula_weight	19811.9 kDa
EC 编号 ec_number	2.7.13.3
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2606

DGSLQLELGTFNLHTLFREVLNLIKPIAVVKKLPITLNLAPDLPEFVVGDEKRLMQIILNIVGNAVKFSKQGSISVTALVTKSDTRAADFFVVPTGSHFYLRVKVKDSGAGINPQDIPKIFTKFAQTQSLATRSSGGSGLGLAISKRFVNLMEGNIWIESDGLGKGCTAIFDVKLGISERSNE

来源 Source

来源生物 organism	Arabidopsis thaliana
通用名 common_name	thale cress
NCBI Class编号 ncbi_taxonomy_id	3702
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	CADMIUM ION
Molecular weight formula_weight	112.4 kDa
Source method src_method	syn
Copy count entity_count	11

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	ACETATE ION
Molecular weight formula_weight	59.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	99

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	4pl9A00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	565 — Heat Shock Protein 90
Homologous superfamily homologous superfamily	10 — Histidine kinase-like ATPase, C-terminal domain

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8. Citations (1)

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Unit-cell length a length_a	76.260 Å
Unit-cell length b length_b	83.120 Å
Unit-cell length c length_c	91.930 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	8

Space group space_group	I 21 21 21
Space-group number int_tables_number	24
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	41.560 Å
R factor r_factor	0.1483
R_work r_work	0.1465
R_free r_free	0.1816

fit	/app/data/saxs_computation/pl/4pl9/4pl9.fit
pddf	/app/data/pr_computation/pl/4pl9/4pl9.pr.out
profile	/app/data/saxs_computation/pl/4pl9/4pl9.dat

Structure of the catalytic domain of ETR1 from Arabidopsis thaliana

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

Ethylene receptor 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

Refinement Refinement

Diffraction experiment Diffraction