5a6u

Native mammalian ribosome-bound Sec61 protein-conducting channel in the 'non-inserting' state

Method: ELECTRON MICROSCOPY Dmax: 85.1 Å Quality: REASONABLE

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

SEC61A

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 26–476 Fragment:UNP RESIDUES 26-476 SEC61B × 1 (P60467) SEC61G × 1 (P60058) ELECTRON MICROSCOPY cryo-EM buffer:20MM HEPES, 50MM KCL, 2MM MGCL2;pH 7.6;20MM HEPES, 50MM KCL, 2MM MGCL2 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;VITRIFICATION 1 -- CRYOGEN- ETHANE-PROPANE MIXTURE, HUMIDITY- 70, INSTRUMENT- FEI VITROBOT MARK IV, METHOD- BLOT 3 SECONDS BEFORE PLUNGING., Resolution 9.00 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.

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 A; PDBConstruct 1–451; UniProt 26–476

SEC61B

OrganismNot specified

UniProt P60467

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 61–96 Fragment:UNP RESIDUES 61-96 SEC61A × 1 (P38377) SEC61G × 1 (P60058) ELECTRON MICROSCOPY cryo-EM buffer:20MM HEPES, 50MM KCL, 2MM MGCL2;pH 7.6;20MM HEPES, 50MM KCL, 2MM MGCL2 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;VITRIFICATION 1 -- CRYOGEN- ETHANE-PROPANE MIXTURE, HUMIDITY- 70, INSTRUMENT- FEI VITROBOT MARK IV, METHOD- BLOT 3 SECONDS BEFORE PLUNGING., Resolution 9.00 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SC61B_CANFA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–36; UniProt 61–96

SEC61G

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 7–68 Fragment:UNP RESIDUES 7-68 SEC61A × 1 (P38377) SEC61B × 1 (P60467) ELECTRON MICROSCOPY cryo-EM buffer:20MM HEPES, 50MM KCL, 2MM MGCL2;pH 7.6;20MM HEPES, 50MM KCL, 2MM MGCL2 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;VITRIFICATION 1 -- CRYOGEN- ETHANE-PROPANE MIXTURE, HUMIDITY- 70, INSTRUMENT- FEI VITROBOT MARK IV, METHOD- BLOT 3 SECONDS BEFORE PLUNGING., Resolution 9.00 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.

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 3
Chains and sequence ranges Author chain G; PDBConstruct 1–62; UniProt 7–68

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 5a6u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5a6u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5a6u
Deposition date deposition_date2015-07-01
Structure title titleNative mammalian ribosome-bound Sec61 protein-conducting channel in the 'non-inserting' state
Keywords keywordsTRANSLATION, RIBOSOME, SEC61, TRANSLOCON, ENDOPLASMIC RETICULUM, CRYOELECTRON TOMOGRAPHY, SUBTOMOGRAM ANALYSIS; TRANSLATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier26.63
Radius of gyration Rg (electron density) rg_electron25.48
Forward intensity I(0) i043326500.00
Molecular weight molecular_weight53603.0 kDa
Excluded volume excluded_volume68468 ų
Envelope volume envelope_volume93726 ų
Hydration-shell volume shell_volume30796 ų
Envelope diameter envelope_diameter88.9
Shell Rg shell_rg32.51
Envelope Rg envelope_rg25.49
Shape Rg shape_rg25.46
Total Rg total_rg26.46
Total atoms total_atoms7770
Residues n_residues494
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 dmax85.1
Rg (real space) rg_real26.53
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real4.3330e+07
I(0) uncertainty (real space) i0_real_error5.7010e+05
Rg (reciprocal space) rg_reciprocal26.56
I(0) (reciprocal space) i0_reciprocal43330000.0000
Solution quality estimate total_estimate0.6944
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.0
Skewness Skewness skewness0.246
Kurtosis Kurtosis kurtosis-0.243
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4611000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 0.145; Positv: 1.000; Valcen: 0.997; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)