SAXSdb — 9vvj

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

Erlin-1

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Heteromer Protein × 26 其他Polymer 26 PDB declaration: 26-meric（26） Consistent with protein copy count	Chain A； UniProt 6–309 Chain B； UniProt 6–309 Chain C； UniProt 6–309 Chain D； UniProt 6–309 Chain E； UniProt 6–309 Chain F； UniProt 6–309 Chain G； UniProt 6–309 Chain H； UniProt 6–309 Chain I； UniProt 6–309 Chain J； UniProt 6–309 Chain K； UniProt 6–309 Chain L； UniProt 6–309 Chain M； UniProt 6–309	Not recorded	Erlin-2 × 13 （O94905） 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 26	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.60 Å

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 9VVJ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9O9U The Erlin1/2 complex Deposited 2025-04-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 26 PDB declaration: 26-meric	Chain A 3–348（346 aa） Chain B 3–348（346 aa） Chain C 3–348（346 aa） Chain D 3–348（346 aa） Chain E 3–348（346 aa） Chain F 3–348（346 aa） Chain G 3–348（346 aa） Chain H 3–348（346 aa） Chain I 3–348（346 aa） Chain J 3–348（346 aa） Chain K 3–348（346 aa） Chain L 3–348（346 aa） Chain M 3–348（346 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
9VVG Cryo-EM structure of the erlin1/2 complex purified using GDN and CHS Deposited 2025-07-15	Different construct Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 26 PDB declaration: 26-meric	Chain A 13–309（297 aa） Chain B 13–309（297 aa） Chain C 13–309（297 aa） Chain D 13–309（297 aa） Chain E 13–309（297 aa） Chain F 13–309（297 aa） Chain G 13–309（297 aa） Chain H 13–309（297 aa） Chain I 13–309（297 aa） Chain J 13–309（297 aa） Chain K 13–309（297 aa） Chain L 13–309（297 aa） Chain M 13–309（297 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ERLN1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–304； UniProt 6–309 Author chain B； PDBConstruct 1–304； UniProt 6–309 Author chain C； PDBConstruct 1–304； UniProt 6–309 Author chain D； PDBConstruct 1–304； UniProt 6–309 Author chain E； PDBConstruct 1–304； UniProt 6–309 Author chain F； PDBConstruct 1–304； UniProt 6–309 Author chain G； PDBConstruct 1–304； UniProt 6–309 Author chain H； PDBConstruct 1–304； UniProt 6–309 Author chain I； PDBConstruct 1–304； UniProt 6–309 Author chain J； PDBConstruct 1–304； UniProt 6–309 Author chain K； PDBConstruct 1–304； UniProt 6–309 Author chain L； PDBConstruct 1–304； UniProt 6–309 Author chain M； PDBConstruct 1–304； UniProt 6–309

Erlin-2

Homo sapiens

UniProt O94905

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Heteromer Protein × 26 其他Polymer 26 PDB declaration: 26-meric（26） Consistent with protein copy count	Chain a； UniProt 4–307 Chain b； UniProt 4–307 Chain c； UniProt 4–307 Chain d； UniProt 4–307 Chain e； UniProt 4–307 Chain f； UniProt 4–307 Chain g； UniProt 4–307 Chain h； UniProt 4–307 Chain i； UniProt 4–307 Chain j； UniProt 4–307 Chain k； UniProt 4–307 Chain l； UniProt 4–307 Chain m； UniProt 4–307	Not recorded	Erlin-1 × 13 （O75477） 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 26	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.60 Å

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 9VVJ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9O9U The Erlin1/2 complex Deposited 2025-04-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 26 PDB declaration: 26-meric	Chain a 1–339（339 aa） Chain b 1–339（339 aa） Chain c 1–339（339 aa） Chain d 1–339（339 aa） Chain e 1–339（339 aa） Chain f 1–339（339 aa） Chain g 1–339（339 aa） Chain h 1–339（339 aa） Chain i 1–339（339 aa） Chain j 1–339（339 aa） Chain k 1–339（339 aa） Chain l 1–339（339 aa） Chain m 1–339（339 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
9VVG Cryo-EM structure of the erlin1/2 complex purified using GDN and CHS Deposited 2025-07-15	Different construct Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 26 PDB declaration: 26-meric	Chain a 10–308（299 aa） Chain b 10–308（299 aa） Chain c 10–308（299 aa） Chain d 10–308（299 aa） Chain e 10–308（299 aa） Chain f 10–308（299 aa） Chain g 10–308（299 aa） Chain h 10–308（299 aa） Chain i 10–308（299 aa） Chain j 10–308（299 aa） Chain k 10–308（299 aa） Chain l 10–308（299 aa） Chain m 10–308（299 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
9WFF Cryo-EM structure of the human Erlin2 oligomer Deposited 2025-08-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 26 PDB declaration: 26-meric	Chain A 21–299（279 aa） Chain B 21–299（279 aa） Chain C 21–299（279 aa） Chain D 21–299（279 aa） Chain E 21–299（279 aa） Chain F 21–299（279 aa） Chain G 21–299（279 aa） Chain H 21–299（279 aa） Chain I 21–299（279 aa） Chain J 21–299（279 aa） Chain K 21–299（279 aa） Chain L 21–299（279 aa） Chain M 21–299（279 aa） Chain N 21–299（279 aa） Chain O 21–299（279 aa） Chain P 21–299（279 aa） Chain Q 21–299（279 aa） Chain R 21–299（279 aa） Chain S 21–299（279 aa） Chain T 21–299（279 aa） Chain U 21–299（279 aa） Chain V 21–299（279 aa） Chain W 21–299（279 aa） Chain X 21–299（279 aa） Chain Y 21–299（279 aa） Chain Z 21–299（279 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.12 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ERLN2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain a； PDBConstruct 1–304； UniProt 4–307 Author chain b； PDBConstruct 1–304； UniProt 4–307 Author chain c； PDBConstruct 1–304； UniProt 4–307 Author chain d； PDBConstruct 1–304； UniProt 4–307 Author chain e； PDBConstruct 1–304； UniProt 4–307 Author chain f； PDBConstruct 1–304； UniProt 4–307 Author chain g； PDBConstruct 1–304； UniProt 4–307 Author chain h； PDBConstruct 1–304； UniProt 4–307 Author chain i； PDBConstruct 1–304； UniProt 4–307 Author chain j； PDBConstruct 1–304； UniProt 4–307 Author chain k； PDBConstruct 1–304； UniProt 4–307 Author chain l； PDBConstruct 1–304； UniProt 4–307 Author chain m； PDBConstruct 1–304； UniProt 4–307

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	9vvj
Deposition date deposition_date	2025-07-15
Structure title title	Cryo-EM structure of the erlin1/2 complex purified using DDM and GDN
Keywords keywords	Cryo-EM, complex, MEMBRANE PROTEIN, SPFH protein family; MEMBRANE PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	94.75 Å
Radius of gyration Rg (electron density) rg_electron	94.32 Å
Forward intensity I(0) i0	10329400000.00
Molecular weight molecular_weight	901440.0 kDa
Excluded volume excluded_volume	1143800 Å³
Envelope volume envelope_volume	3114900 Å³
Hydration-shell volume shell_volume	283720 Å³
Envelope diameter envelope_diameter	236.4 Å
Shell Rg shell_rg	98.51 Å
Envelope Rg envelope_rg	83.29 Å
Shape Rg shape_rg	94.37 Å
Total Rg total_rg	94.17 Å
Total atoms total_atoms	63388
Residues n_residues	7904
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	246.5 Å
Rg (real space) rg_real	93.71 Å
Rg uncertainty (real space) rg_real_error	0.74 Å
I(0) (real space) i0_real	1.0320e+10
I(0) uncertainty (real space) i0_real_error	2.0330e+08
Rg (reciprocal space) rg_reciprocal	97.91 Å
I(0) (reciprocal space) i0_reciprocal	10440000000.0000
Solution quality estimate total_estimate	0.8406
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	154.0 Å
Skewness Skewness skewness	-0.282
Kurtosis Kurtosis kurtosis	-0.770
Angular range angular_range	— – 0.0800 Å⁻¹
Current regularization parameter α current_alpha	0.0481
Highest regularization parameter α highest_alpha	343100000.0000
Real-space data points n_real_points	17
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.979; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Erlin-1
Molecular weight formula_weight	34461.8 kDa
Source method src_method	man
Copy count entity_count	13

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,M,L,K,F,E,D,C,B,J,I,H,G
Atom count atom_count	63388

ARVLVAAVVGLVAVLLYASIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAVFDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNLMAPGLTIQAVRVTKPKIPEAIRRNFELMEAEKTKLLIAAQKQKVVEKEAETERKKAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADAEYYAAHKYATSNKHKLTPEYLELKKYQAIASNSKIYFGSNIPNMFVD

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	Erlin-2
Molecular weight formula_weight	34188.5 kDa
Source method src_method	man
Copy count entity_count	13

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	a,m,k,l,f,d,b,c,e,i,g,h,j

LGAVVAVASSFFCASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFLVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNIPEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTAMKIAEANKLKLTPEYLQLMKYKAIASNSKMYFGKDIPNMFMD

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 3 Entity 3 branched

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	424.4 kDa
Source method src_method	man
Copy count entity_count	26

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8. Citations (1)

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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	—

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

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	2.60 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	25074

fit	/app/data/saxs_computation/vv/9vvj/9vvj.fit
pddf	/app/data/pr_computation/vv/9vvj/9vvj.pr.out
profile	/app/data/saxs_computation/vv/9vvj/9vvj.dat

Cryo-EM structure of the erlin1/2 complex purified using DDM and GDN

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

Erlin-1

State in the Current Structure

Other States of the Same Protein in the Database

Erlin-2

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 branched

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)