SAXSdb — 8yn0

▼

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

Protein 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 3	Senescence-associated carboxylesterase 101 × 1 （Q4F883） Probable disease resistance protein At5g66890 × 1 （Q9FKZ2） ADENOSINE-5-DIPHOSPHORIBOSE × 1 ADENOSINE-5'-TRIPHOSPHATE × 1 water × 3	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Senescence-associated carboxylesterase 101 × 1 （Q4F883） Probable disease resistance protein At5g66890 × 1 （Q9FKZ2） ADENOSINE-5-DIPHOSPHORIBOSE × 1 ADENOSINE-5'-TRIPHOSPHATE × 1 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	EDS1C_ARATH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–617； UniProt 2–618 Author chain B； PDBConstruct 1–617； UniProt 2–618

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 3	Protein EDS1 × 1 （Q9SU72） Probable disease resistance protein At5g66890 × 1 （Q9FKZ2） ADENOSINE-5-DIPHOSPHORIBOSE × 1 ADENOSINE-5'-TRIPHOSPHATE × 1 water × 3	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Protein EDS1 × 1 （Q9SU72） Probable disease resistance protein At5g66890 × 1 （Q9FKZ2） ADENOSINE-5-DIPHOSPHORIBOSE × 1 ADENOSINE-5'-TRIPHOSPHATE × 1 water × 3	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 C； PDBConstruct 1–536； UniProt 2–537 Author chain E； PDBConstruct 1–536； UniProt 2–537

Probable disease resistance protein At5g66890

Arabidopsis thaliana

UniProt Q9FKZ2

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Protein EDS1 × 1 （Q9SU72） Senescence-associated carboxylesterase 101 × 1 （Q4F883） ADENOSINE-5-DIPHOSPHORIBOSE × 1 ADENOSINE-5'-TRIPHOSPHATE × 1 water × 3	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Protein EDS1 × 1 （Q9SU72） Senescence-associated carboxylesterase 101 × 1 （Q4F883） ADENOSINE-5-DIPHOSPHORIBOSE × 1 ADENOSINE-5'-TRIPHOSPHATE × 1 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	DRL41_ARATH
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain D； PDBConstruct 1–415； UniProt 1–415 Author chain H； PDBConstruct 1–415； UniProt 1–415

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	8yn0
Deposition date deposition_date	2024-03-10
Structure title title	Crystal structure of NRG1C in complex with EDS1-SAG101-(ADPr-ATP)
Keywords keywords	EDS1, SAG101, ATP-ADPR, NRG1C, PLANT PROTEIN, PLANT PROTEIN-HYDROLASE complex; PLANT PROTEIN/HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

▼

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.

8yn0__assembly_1__model_1

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

Download this curve (.dat)

8yn0__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

8yn0__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	40.00 Å
Rg (electron density)	39.66 Å
Total Rg	39.91 Å
Atom count	12703
Residues	1556
Excluded volume	226210 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`8yn0__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`8yn0__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Protein EDS1
Molecular weight formula_weight	71093.4 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,A
Atom count atom_count	26107

AFEALTGINGDLITRSWSASKQAYLTERYHKEEAGAVVIFAFQPSFSEKDFFDPDNKSSFGEIKLNRVQFPCMRKIGKGDVATVNEAFLKNLEAIIDPRTSFQASVEMAVRSRKQIVFTGHSSGGATAILATVWYLEKYFIRNPNVYLEPRCVTFGAPLVGDSIFSHALGREKWSRFFVNFVSRFDIVPRIMLARKASVEETLPHVLAQLDPRKSSVQESEQRITEFYTRVMRDTSTVANQAVCELTGSAEAFLETLSSFLELSPYRPAGTFVFSTEKRLVAVNNSDAILQMLFYTSQASDEQEWSLIPFRSIRDHHSYEELVQSMGKKLFNHLDGENSIESTLNDLGVSTRGRQYVQAALEEEKKRVENQKKIIQVIEQERFLKKLAWIEDEYKPKCQAHKNGYYDSFKVSNEENDFKANVKRAELAGVFDEVLGLMKKCQLPDEFEGDIDWIKLATRYRRLVEPLDIANYHRHLKNEDTGPYMKRGRPTRYIYAQRGYEHYILKPNGMIAEDVFWNKVNGLNLGLQLEEIQETLKNSGSECGSCFWAEVEELKGKPYEEVEVRVKTLEGMLGEWITDGEVDDKEIFLEGSTFRKWWITLPKNHKSHSPLRDYMMD

Source Source

Source organism organism	Arabidopsis thaliana
Common name common_name	thale cress
NCBI taxonomy ID ncbi_taxonomy_id	3702
Host organism host_organism	Spodoptera frugiperda

Entity 2 Entity 2 polymer

Description description	Senescence-associated carboxylesterase 101
Molecular weight formula_weight	62022.2 kDa
EC 编号 ec_number	3.1.1.1
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,C

ESSSSLKGSALGKLVVTSGLLHSSWSKILEIHNPPYSNHDPGLQVSKKKKDSGLEFQIHREEKFTLVVFSAPPICRSSSSDSTLLHVKDKENPFPFLCSENNPSFSLHTPAFNLFTSASTSLTYLKSELLQTLKSEKPVIITGAALGGSVASLYTLWLLETIEPTLKRPLCITFGSPLIGDASLQQILENSVRNSCFLHVVSAQTRIKMDFFKPFGTFLICFDSGCVCIEDHVAVTELLNGVHDSGLVDYSQVLNRLDQSMLSLADSRLIPEDVIKGIEKRAEMKNLRFDMMFKKLNDMKISMAYIEWYKKKCKEVKIGYYDRFKTQLAFPSKEFDINIKNHHKSELNRFWKSVVEEVERRPQSDASILKRRFLFSGNNYRRMIEPLDIAEYYLEGRKEYRTTGRSHHYVMLEKWFGMESILIEKERCKKRDLSDLLTFDSCFWAEVEDSLIVINQLNTTVGMRDDVREVLTRKLVEFEGYVWEIITKREVSPEIFLEESSFMKWWKEYKKIKGFNSSYLTEFMNTRKYESYGKSQ

Source Source

Source organism organism	Arabidopsis thaliana
Common name common_name	thale cress
NCBI taxonomy ID ncbi_taxonomy_id	3702
Host organism host_organism	Spodoptera frugiperda

Entity 3 Entity 3 polymer

Description description	Probable disease resistance protein At5g66890
Molecular weight formula_weight	47602.7 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,D

MNSNSIQSFDALPHNLRECFLDMASFLEDQRIIASTIIDLWSASYGKEGMNNLQDLASRNLLKLLPIGRNEYEDGFYNELLVKQDNVLREFAINQCLKESSSIFERKRLNLEIQDNKFPNWCLNPKQPIVINASLFSISTDDSFASSWFEMDCPNVEALVLNISSSNYALPNFIATMKELKVVIIINHGLEPAKLTNLSCLSSLPNLKRIRFEKVSISLLDIPKLGLKSLEKLSLWFCHVVDALNELEDVSETLQSLQEIEIDYCYNLDELPYWISQVVSLKKLSVTNCNKLCRVIEAIGDLRDLETLRLSSCASLLELPETIDRLDNLRFLDVSGGFQLKNLPLEIGKLKKLEKISMKDCYRCELPDSVKNLENLEVKCDEDTAFLWKILKPEMKNLTITEEKTEHNLNLLQLF

Source Source

Source organism organism	Arabidopsis thaliana
Common name common_name	thale cress
NCBI taxonomy ID ncbi_taxonomy_id	3702
Host organism host_organism	Spodoptera frugiperda

Entity 4 Entity 4 non-polymer

Description description	ADENOSINE-5-DIPHOSPHORIBOSE
Molecular weight formula_weight	559.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	ADENOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	507.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	704

▶

Unit-cell length a length_a	91.521 Å
Unit-cell length b length_b	154.914 Å
Unit-cell length c length_c	171.110 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	89.69 °
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	2.490 Å
Low-resolution limit resolution_low	39.770 Å
R factor r_factor	0.1991
R_work r_work	0.1986
R_free r_free	0.2379

Crystal structure of NRG1C in complex with EDS1-SAG101-(ADPr-ATP)

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

Protein 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

Probable disease resistance protein At5g66890

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

8yn0__assembly_1__model_1

8yn0__assembly_1__model_1 | I(q)

8yn0__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 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

7. Citations (1)

Crystal structure of NRG1C in complex with EDS1-SAG101-(ADPr-ATP)

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

Protein 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

Probable disease resistance protein At5g66890

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

8yn0__assembly_1__model_1

8yn0__assembly_1__model_1 | I(q)

8yn0__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 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

7. Citations (1)