7adp

Cryo-EM structure of human ER membrane protein complex in GDN detergent

Method: ELECTRON MICROSCOPY Dmax: 191.2 Å Quality: REASONABLE

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

ER membrane protein complex subunit 1

Homo sapiens

UniProt Q8N766

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–993 Not recorded ER membrane protein complex subunit 2 × 1 (Q15006) ER membrane protein complex subunit 3 × 1 (Q9P0I2) ER membrane protein complex subunit 4 × 1 (Q5J8M3) Membrane magnesium transporter 1 × 1 (Q8N4V1) ER membrane protein complex subunit 6 × 1 (Q9BV81) ER membrane protein complex subunit 8 × 1 (O43402) ER membrane protein complex subunit 10 × 1 (Q5UCC4) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 6;10 mM ammonium citrate pH 6.0, 100 mM sodium chloride, 0.25 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EMC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–993; UniProt 1–993

ER membrane protein complex subunit 2

Homo sapiens

UniProt Q15006

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–297 Not recorded ER membrane protein complex subunit 1 × 1 (Q8N766) ER membrane protein complex subunit 3 × 1 (Q9P0I2) ER membrane protein complex subunit 4 × 1 (Q5J8M3) Membrane magnesium transporter 1 × 1 (Q8N4V1) ER membrane protein complex subunit 6 × 1 (Q9BV81) ER membrane protein complex subunit 8 × 1 (O43402) ER membrane protein complex subunit 10 × 1 (Q5UCC4) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 6;10 mM ammonium citrate pH 6.0, 100 mM sodium chloride, 0.25 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EMC2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–297; UniProt 1–297

ER membrane protein complex subunit 3

Homo sapiens

UniProt Q9P0I2

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 1–261 Not recorded ER membrane protein complex subunit 1 × 1 (Q8N766) ER membrane protein complex subunit 2 × 1 (Q15006) ER membrane protein complex subunit 4 × 1 (Q5J8M3) Membrane magnesium transporter 1 × 1 (Q8N4V1) ER membrane protein complex subunit 6 × 1 (Q9BV81) ER membrane protein complex subunit 8 × 1 (O43402) ER membrane protein complex subunit 10 × 1 (Q5UCC4) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 6;10 mM ammonium citrate pH 6.0, 100 mM sodium chloride, 0.25 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EMC3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–261; UniProt 1–261

ER membrane protein complex subunit 4

Homo sapiens

UniProt Q5J8M3

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain D; UniProt 1–183 Not recorded ER membrane protein complex subunit 1 × 1 (Q8N766) ER membrane protein complex subunit 2 × 1 (Q15006) ER membrane protein complex subunit 3 × 1 (Q9P0I2) Membrane magnesium transporter 1 × 1 (Q8N4V1) ER membrane protein complex subunit 6 × 1 (Q9BV81) ER membrane protein complex subunit 8 × 1 (O43402) ER membrane protein complex subunit 10 × 1 (Q5UCC4) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 6;10 mM ammonium citrate pH 6.0, 100 mM sodium chloride, 0.25 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EMC4_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–183; UniProt 1–183

Membrane magnesium transporter 1

Homo sapiens

UniProt Q8N4V1

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–131 Not recorded ER membrane protein complex subunit 1 × 1 (Q8N766) ER membrane protein complex subunit 2 × 1 (Q15006) ER membrane protein complex subunit 3 × 1 (Q9P0I2) ER membrane protein complex subunit 4 × 1 (Q5J8M3) ER membrane protein complex subunit 6 × 1 (Q9BV81) ER membrane protein complex subunit 8 × 1 (O43402) ER membrane protein complex subunit 10 × 1 (Q5UCC4) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 6;10 mM ammonium citrate pH 6.0, 100 mM sodium chloride, 0.25 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MMGT1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–131; UniProt 1–131

ER membrane protein complex subunit 6

Homo sapiens

UniProt Q9BV81

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain F; UniProt 1–110 Not recorded ER membrane protein complex subunit 1 × 1 (Q8N766) ER membrane protein complex subunit 2 × 1 (Q15006) ER membrane protein complex subunit 3 × 1 (Q9P0I2) ER membrane protein complex subunit 4 × 1 (Q5J8M3) Membrane magnesium transporter 1 × 1 (Q8N4V1) ER membrane protein complex subunit 8 × 1 (O43402) ER membrane protein complex subunit 10 × 1 (Q5UCC4) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 6;10 mM ammonium citrate pH 6.0, 100 mM sodium chloride, 0.25 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EMC6_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–110; UniProt 1–110

ER membrane protein complex subunit 8

Homo sapiens

UniProt O43402

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain H; UniProt 1–210 Not recorded ER membrane protein complex subunit 1 × 1 (Q8N766) ER membrane protein complex subunit 2 × 1 (Q15006) ER membrane protein complex subunit 3 × 1 (Q9P0I2) ER membrane protein complex subunit 4 × 1 (Q5J8M3) Membrane magnesium transporter 1 × 1 (Q8N4V1) ER membrane protein complex subunit 6 × 1 (Q9BV81) ER membrane protein complex subunit 10 × 1 (Q5UCC4) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 6;10 mM ammonium citrate pH 6.0, 100 mM sodium chloride, 0.25 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EMC8_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain H; PDBConstruct 1–210; UniProt 1–210

ER membrane protein complex subunit 10

Homo sapiens

UniProt Q5UCC4

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain I; UniProt 2–262 Not recorded ER membrane protein complex subunit 1 × 1 (Q8N766) ER membrane protein complex subunit 2 × 1 (Q15006) ER membrane protein complex subunit 3 × 1 (Q9P0I2) ER membrane protein complex subunit 4 × 1 (Q5J8M3) Membrane magnesium transporter 1 × 1 (Q8N4V1) ER membrane protein complex subunit 6 × 1 (Q9BV81) ER membrane protein complex subunit 8 × 1 (O43402) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 6;10 mM ammonium citrate pH 6.0, 100 mM sodium chloride, 0.25 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EMC10_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain I; PDBConstruct 3–263; UniProt 2–262

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.

SAXS scattering curve SAXS Profile

SAXS profile for 7adp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7adp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7adp
Deposition date deposition_date2020-09-15
Structure title titleCryo-EM structure of human ER membrane protein complex in GDN detergent
Keywords keywordsER membrane protein, EMC, Membrane protein biogenesis, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.17
Radius of gyration Rg (electron density) rg_electron60.54
Forward intensity I(0) i0618102000.00
Molecular weight molecular_weight212940.0 kDa
Excluded volume excluded_volume268960 ų
Envelope volume envelope_volume419760 ų
Hydration-shell volume shell_volume64392 ų
Envelope diameter envelope_diameter203.9
Shell Rg shell_rg52.36
Envelope Rg envelope_rg58.67
Shape Rg shape_rg60.55
Total Rg total_rg60.24
Total atoms total_atoms15026
Residues n_residues1880
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax191.2
Rg (real space) rg_real60.90
Rg uncertainty (real space) rg_real_error2.02
I(0) (real space) i0_real6.1810e+08
I(0) uncertainty (real space) i0_real_error1.2370e+07
Rg (reciprocal space) rg_reciprocal59.47
I(0) (reciprocal space) i0_reciprocal616600000.0000
Solution quality estimate total_estimate0.7495
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary44.1
Skewness Skewness skewness0.425
Kurtosis Kurtosis kurtosis-0.778
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40340000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.655; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.762; Smooth: 0.013

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)