SAXSdb — 9o9u

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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	Protein heterocomplex Heteromer Protein × 26 PDB declaration: 26-meric（26） Consistent with protein copy count	Chain A； UniProt 3–348 Chain B； UniProt 3–348 Chain C； UniProt 3–348 Chain D； UniProt 3–348 Chain E； UniProt 3–348 Chain F； UniProt 3–348 Chain G； UniProt 3–348 Chain H； UniProt 3–348 Chain I； UniProt 3–348 Chain J； UniProt 3–348 Chain K； UniProt 3–348 Chain L； UniProt 3–348 Chain M； UniProt 3–348	Not recorded	Erlin-2 × 13 （O94905） 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

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 9O9U	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9VVG Cryo-EM structure of the erlin1/2 complex purified using GDN and CHS Deposited 2025-07-15	Different construct Different oligomeric state Different ligand/ion Different experimental conditions 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
9VVJ Cryo-EM structure of the erlin1/2 complex purified using DDM and GDN Deposited 2025-07-15	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 26 PDB declaration: 26-meric	Chain A 6–309（304 aa） Chain B 6–309（304 aa） Chain C 6–309（304 aa） Chain D 6–309（304 aa） Chain E 6–309（304 aa） Chain F 6–309（304 aa） Chain G 6–309（304 aa） Chain H 6–309（304 aa） Chain I 6–309（304 aa） Chain J 6–309（304 aa） Chain K 6–309（304 aa） Chain L 6–309（304 aa） Chain M 6–309（304 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 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 36–381； UniProt 3–348 Author chain B； PDBConstruct 36–381； UniProt 3–348 Author chain C； PDBConstruct 36–381； UniProt 3–348 Author chain D； PDBConstruct 36–381； UniProt 3–348 Author chain E； PDBConstruct 36–381； UniProt 3–348 Author chain F； PDBConstruct 36–381； UniProt 3–348 Author chain G； PDBConstruct 36–381； UniProt 3–348 Author chain H； PDBConstruct 36–381； UniProt 3–348 Author chain I； PDBConstruct 36–381； UniProt 3–348 Author chain J； PDBConstruct 36–381； UniProt 3–348 Author chain K； PDBConstruct 36–381； UniProt 3–348 Author chain L； PDBConstruct 36–381； UniProt 3–348 Author chain M； PDBConstruct 36–381； UniProt 3–348

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	Protein heterocomplex Heteromer Protein × 26 PDB declaration: 26-meric（26） Consistent with protein copy count	Chain a； UniProt 1–339 Chain b； UniProt 1–339 Chain c； UniProt 1–339 Chain d； UniProt 1–339 Chain e； UniProt 1–339 Chain f； UniProt 1–339 Chain g； UniProt 1–339 Chain h； UniProt 1–339 Chain i； UniProt 1–339 Chain j； UniProt 1–339 Chain k； UniProt 1–339 Chain l； UniProt 1–339 Chain m； UniProt 1–339	Not recorded	Erlin-1 × 13 （O75477） 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

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 9O9U	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9VVG Cryo-EM structure of the erlin1/2 complex purified using GDN and CHS Deposited 2025-07-15	Different construct Different oligomeric state Different ligand/ion Different experimental conditions 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
9VVJ Cryo-EM structure of the erlin1/2 complex purified using DDM and GDN Deposited 2025-07-15	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 26 PDB declaration: 26-meric	Chain a 4–307（304 aa） Chain b 4–307（304 aa） Chain c 4–307（304 aa） Chain d 4–307（304 aa） Chain e 4–307（304 aa） Chain f 4–307（304 aa） Chain g 4–307（304 aa） Chain h 4–307（304 aa） Chain i 4–307（304 aa） Chain j 4–307（304 aa） Chain k 4–307（304 aa） Chain l 4–307（304 aa） Chain m 4–307（304 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å
9WFF Cryo-EM structure of the human Erlin2 oligomer Deposited 2025-08-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions 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 1–339； UniProt 1–339 Author chain b； PDBConstruct 1–339； UniProt 1–339 Author chain c； PDBConstruct 1–339； UniProt 1–339 Author chain d； PDBConstruct 1–339； UniProt 1–339 Author chain e； PDBConstruct 1–339； UniProt 1–339 Author chain f； PDBConstruct 1–339； UniProt 1–339 Author chain g； PDBConstruct 1–339； UniProt 1–339 Author chain h； PDBConstruct 1–339； UniProt 1–339 Author chain i； PDBConstruct 1–339； UniProt 1–339 Author chain j； PDBConstruct 1–339； UniProt 1–339 Author chain k； PDBConstruct 1–339； UniProt 1–339 Author chain l； PDBConstruct 1–339； UniProt 1–339 Author chain m； PDBConstruct 1–339； UniProt 1–339

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	9o9u
Deposition date deposition_date	2025-04-18
Structure title title	The Erlin1/2 complex
Keywords keywords	SPFH, ER, Erlin1, Erlin2, MEMBRANE PROTEIN; 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	93.19 Å
Radius of gyration Rg (electron density) rg_electron	92.68 Å
Forward intensity I(0) i0	9510320000.00
Molecular weight molecular_weight	862820.0 kDa
Excluded volume excluded_volume	1093900 Å³
Envelope volume envelope_volume	2772100 Å³
Hydration-shell volume shell_volume	260090 Å³
Envelope diameter envelope_diameter	237.3 Å
Shell Rg shell_rg	95.81 Å
Envelope Rg envelope_rg	81.17 Å
Shape Rg shape_rg	92.75 Å
Total Rg total_rg	92.47 Å
Total atoms total_atoms	60697
Residues n_residues	7553
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	252.5 Å
Rg (real space) rg_real	92.25 Å
Rg uncertainty (real space) rg_real_error	1.01 Å
I(0) (real space) i0_real	9.5050e+09
I(0) uncertainty (real space) i0_real_error	1.7430e+08
Rg (reciprocal space) rg_reciprocal	96.07 Å
I(0) (reciprocal space) i0_reciprocal	9600000000.0000
Solution quality estimate total_estimate	0.8340
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	148.5 Å
Skewness Skewness skewness	-0.264
Kurtosis Kurtosis kurtosis	-0.757
Angular range angular_range	— – 0.0850 Å⁻¹
Current regularization parameter α current_alpha	0.0208
Highest regularization parameter α highest_alpha	296900000.0000
Real-space data points n_real_points	18
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.961; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; 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	42429.4 kDa
Source method src_method	man
Copy count entity_count	13

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M
Atom count atom_count	60697

MSAWSHPQFEKGGGSGGGSGGSAWSHPQFEKGSGSMTQARVLVAAVVGLVAVLLYASIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAVFDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNLMAPGLTIQAVRVTKPKIPEAIRRNFELMEAEKTKLLIAAQKQKVVEKEAETERKKAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADAEYYAAHKYATSNKHKLTPEYLELKKYQAIASNSKIYFGSNIPNMFVDSSCALKYSDIRTGRESSLPSKEALEPSGENVIQNKESTG

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	37884.5 kDa
Source method src_method	man
Copy count entity_count	13

Polymer Polymer

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

MAQLGAVVAVASSFFCASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFLVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNIPEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTAMKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDSAGSVSKQFEGLADKLSFGLEDEPLETATKEN

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 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	syn
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	3.00 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	95469

fit	/app/data/saxs_computation/o9/9o9u/9o9u.fit
pddf	/app/data/pr_computation/o9/9o9u/9o9u.pr.out
profile	/app/data/saxs_computation/o9/9o9u/9o9u.dat

The Erlin1/2 complex

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

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 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)