3jc2

The structure of the mammalian Sec61 channel opened by a signal sequence

Method: ELECTRON MICROSCOPY Dmax: 83.1 Å Quality: GOOD

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

Protein transport protein Sec61 subunit alpha isoform 1

OrganismNot specified

UniProt P38377

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain 1; UniProt 1–476 Not recorded Protein transport protein Sec61 subunit gamma × 1 (P60058) Prolactin × 1 (Q6VMP1) Protein transport protein Sec61 subunit beta × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM HEPES, 200 mM potassium acetate, 15 mM magnesium acetate, 1 mM DTT, 0.25% Digitonin;pH 7.5;50 mM HEPES, 200 mM potassium acetate, 15 mM magnesium acetate, 1 mM DTT, 0.25% Digitonin cryo-EM vitrification conditions:3 uL sample was added to the grid, incubated for 30 seconds at 4 C, blotted for 9 seconds;Cryogen ETHANE;3 uL sample was added to the grid, incubated for 30 seconds at 4 C, blotted for 9 seconds, and then plunged into liquid ethane (FEI VITROBOT). 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name S61A1_CANFA
Isoform
PDB entities 1
Chains and sequence ranges Author chain 1; PDBConstruct 1–476; UniProt 1–476

Protein transport protein Sec61 subunit gamma

OrganismNot specified

UniProt P60058

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain 2; UniProt 7–68 Not recorded Protein transport protein Sec61 subunit alpha isoform 1 × 1 (P38377) Prolactin × 1 (Q6VMP1) Protein transport protein Sec61 subunit beta × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM HEPES, 200 mM potassium acetate, 15 mM magnesium acetate, 1 mM DTT, 0.25% Digitonin;pH 7.5;50 mM HEPES, 200 mM potassium acetate, 15 mM magnesium acetate, 1 mM DTT, 0.25% Digitonin cryo-EM vitrification conditions:3 uL sample was added to the grid, incubated for 30 seconds at 4 C, blotted for 9 seconds;Cryogen ETHANE;3 uL sample was added to the grid, incubated for 30 seconds at 4 C, blotted for 9 seconds, and then plunged into liquid ethane (FEI VITROBOT). 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SC61G_CANFA
Isoform
PDB entities 2
Chains and sequence ranges Author chain 2; PDBConstruct 1–62; UniProt 7–68

Prolactin

Bos taurus

UniProt Q6VMP1

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain w; UniProt 2–20 Not recorded Protein transport protein Sec61 subunit alpha isoform 1 × 1 (P38377) Protein transport protein Sec61 subunit gamma × 1 (P60058) Protein transport protein Sec61 subunit beta × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM HEPES, 200 mM potassium acetate, 15 mM magnesium acetate, 1 mM DTT, 0.25% Digitonin;pH 7.5;50 mM HEPES, 200 mM potassium acetate, 15 mM magnesium acetate, 1 mM DTT, 0.25% Digitonin cryo-EM vitrification conditions:3 uL sample was added to the grid, incubated for 30 seconds at 4 C, blotted for 9 seconds;Cryogen ETHANE;3 uL sample was added to the grid, incubated for 30 seconds at 4 C, blotted for 9 seconds, and then plunged into liquid ethane (FEI VITROBOT). 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q6VMP1_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain w; PDBConstruct 1–19; UniProt 2–20

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 3jc2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3jc2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3jc2
Deposition date deposition_date2015-11-15
Structure title titleThe structure of the mammalian Sec61 channel opened by a signal sequence
Keywords keywordsSec61, translocation, signal sequence, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier26.59
Radius of gyration Rg (electron density) rg_electron25.26
Forward intensity I(0) i044269900.00
Molecular weight molecular_weight55526.0 kDa
Excluded volume excluded_volume71537 ų
Envelope volume envelope_volume98330 ų
Hydration-shell volume shell_volume31856 ų
Envelope diameter envelope_diameter86.5
Shell Rg shell_rg33.13
Envelope Rg envelope_rg25.23
Shape Rg shape_rg25.26
Total Rg total_rg26.31
Total atoms total_atoms3911
Residues n_residues514
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 dmax83.1
Rg (real space) rg_real26.43
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real4.4270e+07
I(0) uncertainty (real space) i0_real_error6.1370e+05
Rg (reciprocal space) rg_reciprocal26.48
I(0) (reciprocal space) i0_reciprocal44270000.0000
Solution quality estimate total_estimate0.8951
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.6
Skewness Skewness skewness0.157
Kurtosis Kurtosis kurtosis-0.357
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4577000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.882; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id3jc2200
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily820 — Preprotein translocase SecE subunit

8. Citations (1)

9. Files and Curves (10)