SAXSdb — 4nfu

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

EDS1

Arabidopsis thaliana

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Senescence-associated carboxylesterase 101 × 1 （Q4F883） beta-D-glucopyranose × 1 ISOPROPYL ALCOHOL × 3 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9XF23_ARATH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 15–636； UniProt 2–623

Senescence-associated carboxylesterase 101

Arabidopsis thaliana

UniProt Q4F883

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	EDS1 × 1 （Q9XF23） beta-D-glucopyranose × 1 ISOPROPYL ALCOHOL × 3 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SG101_ARATH
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 5–540； UniProt 1–536

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	4nfu
Deposition date deposition_date	2013-11-01
Structure title title	Structure of the central plant immunity signaling node EDS1 in complex with its interaction partner SAG101
Keywords keywords	alpha/beta hydrolase fold, innate immunity, pathogen defense, Phytoalexin Deficient 4, PAD4, nucleus, hydrolase, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

4nfu__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

4nfu__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4nfu__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	36.42 Å
Rg (electron density)	35.80 Å
Total Rg	36.25 Å
Atom count	9316
Residues	1143
Excluded volume	166160 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4nfu__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	EDS1
Molecular weight formula_weight	73152.6 kDa
EC 编号 ec_number	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	9638

MGSSHHHHHHSQDPAFEALTGINGDLITRSWSASKQAYLTERYHKEEAGAVVIFAFQPSFSEKDFFDPDNKSSFGEIKLNRVQFPCMRKIGKGDVATVNEAFLKNLEAVIDPRTSFQASVEMAVRSRKQIVFTGHSSGGATAILATVWYLEKYFIRNPNVYLEPRCVTFGAPLVGDSIFSHALGREKWSRFFVNFVTRFDIVPRITLARKASVEETLPHVLAQLDPRNSSVQESEQRITEFYTSVMRDTSTVANQAVCELTGSAEAILETLSSFLELSPYRPAGTFVFSTEKRLVAVNNSDAILQMLFYTCQASDEQEWSLIPFRSIRDHHSYEELVQSMGMKLFNHLDGENSIESSLNDLGVSTRGRQYVQAALEEEKKRVENQKKIIQVIQQERFLKKLAWIEDEYKPKCQAHKNGYYDSFKVSNEENDFKANVKRAELAGVFDEVLGLLKKCQLPDEFEGDIDWIKLATRYRRLVEPLDIANYHRHLKNEDTGPYMKRGRPTRYIYAQRGYEHHILKPNGMIAEDVFWNKVNGLNLGLQLEEIQETLKNSGSECGSCFWAEVEELKGKPYEEVEVRVKTLEGMLREWITAGEVDEKEIFLEGSTFRKWWITLPKNHKSHSPLRDYMMDEITDT

Source Source

Source organism organism	Arabidopsis thaliana
Common name common_name	mouse-ear cress
NCBI taxonomy ID ncbi_taxonomy_id	3702
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Senescence-associated carboxylesterase 101
Molecular weight formula_weight	62449.6 kDa
EC 编号 ec_number	3.1.1.1
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

SQDPESSSSLKGSALGKLVVTSGLLHSSWSKILEIHNPPYSNHDPGLQVSKKKKDSGLEFQIHREEKFTLVVFSAPPICRSSSSDSTLLHVKDKENPFPFLCSENNPSFSLHTPAFNLFTSASTSLTYLKSELLQTLKSEKPVIITGAALGGSVASLYTLWLLETIEPTLKRPLCITFGSPLIGDASLQQILENSVRNSCFLHVVSAQTRIKMDFFKPFGTFLICFDSGCVCIEDHVAVTELLNGVHDSGLVDYSQVLNRLDQSMLSLADSRLIPEDVIKGIEKRAEMKNLRFDMMFKKLNDMKISMAYIEWYKKKCKEVKIGYYDRFKTQLAFPSKEFDINIKNHHKSELNRFWKSVVEEVERRPQSDASILKRRFLFSGNNYRRMIEPLDIAEYYLEGRKEYRTTGRSHHYVMLEKWFGMESILIEKERCKKRDLSDLLTFDSCFWAEVEDSLIVINQLNTTVGMRDDVREVLTRKLVEFEGYVWEIITKREVSPEIFLEESSFMKWWKEYKKIKGFNSSYLTEFMNTRKYESYGKSQ

Source Source

Source organism organism	Arabidopsis thaliana
Common name common_name	mouse-ear cress
NCBI taxonomy ID ncbi_taxonomy_id	3702
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	beta-D-glucopyranose
Molecular weight formula_weight	180.2 kDa
Source method src_method	man
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	ISOPROPYL ALCOHOL
Molecular weight formula_weight	60.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 5 Entity 5 non-polymer

Description description	4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
Molecular weight formula_weight	238.3 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	302

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Unit-cell length a length_a	112.586 Å
Unit-cell length b length_b	113.643 Å
Unit-cell length c length_c	125.386 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	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.210 Å
Low-resolution limit resolution_low	34.278 Å
R factor r_factor	0.1768
R_work r_work	0.1764
R_free r_free	0.1955

Structure of the central plant immunity signaling node EDS1 in complex with its interaction partner SAG101

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

EDS1

State in the Current Structure

Other States of the Same Protein in the Database

Senescence-associated carboxylesterase 101

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

4nfu__assembly_1__model_1

4nfu__assembly_1__model_1 | I(q)

4nfu__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

7. Citations (2)

Structure of the central plant immunity signaling node EDS1 in complex with its interaction partner SAG101

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

EDS1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Senescence-associated carboxylesterase 101

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

4nfu__assembly_1__model_1

4nfu__assembly_1__model_1 | I(q)

4nfu__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

7. Citations (2)