4cg7

Cryo-EM of the Sec61-complex bound to the idle 80S ribosome

Method: ELECTRON MICROSCOPY Dmax: 82.2 Å Quality: EXCELLENT

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–476 Not recorded PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT GAMMA × 1 (P60058) TRANSPORT PROTEIN SEC61 SUBUNIT BETA × 1 ELECTRON MICROSCOPY cryo-EM buffer:30 MM HEPES/KOH 7.6, 10 MM MG(OAC)2, 180 MM KOAC/HAC PH 7.6, 0.3 % DIGITONIN, 1 MM DTT;pH 7.6;30 MM HEPES/KOH 7.6, 10 MM MG(OAC)2, 180 MM KOAC/HAC PH 7.6, 0.3 % DIGITONIN, 1 MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 95, INSTRUMENT- FEI VITROBOT MARK IV, METHOD- BLOT FOR 3 SECONDS BEFORE PLUNGING, Resolution 6.90 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 1–476; 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–68 Not recorded PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT ALPHA ISOFORM 1 × 1 (P38377) TRANSPORT PROTEIN SEC61 SUBUNIT BETA × 1 ELECTRON MICROSCOPY cryo-EM buffer:30 MM HEPES/KOH 7.6, 10 MM MG(OAC)2, 180 MM KOAC/HAC PH 7.6, 0.3 % DIGITONIN, 1 MM DTT;pH 7.6;30 MM HEPES/KOH 7.6, 10 MM MG(OAC)2, 180 MM KOAC/HAC PH 7.6, 0.3 % DIGITONIN, 1 MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 95, INSTRUMENT- FEI VITROBOT MARK IV, METHOD- BLOT FOR 3 SECONDS BEFORE PLUNGING, Resolution 6.90 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 B; PDBConstruct 1–68; UniProt 1–68

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 4cg7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4cg7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4cg7
Deposition date deposition_date2013-11-21
Structure title titleCryo-EM of the Sec61-complex bound to the idle 80S ribosome
Keywords keywordsPROTEIN TRANSPORT, CO-TRANSLATIONAL PROTEIN TRANSLOCATION; PROTEIN TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier26.51
Radius of gyration Rg (electron density) rg_electron25.30
Forward intensity I(0) i052199100.00
Molecular weight molecular_weight60421.0 kDa
Excluded volume excluded_volume77692 ų
Envelope volume envelope_volume100600 ų
Hydration-shell volume shell_volume32733 ų
Envelope diameter envelope_diameter85.2
Shell Rg shell_rg33.01
Envelope Rg envelope_rg25.41
Shape Rg shape_rg25.26
Total Rg total_rg26.39
Total atoms total_atoms4252
Residues n_residues550
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 dmax82.2
Rg (real space) rg_real26.39
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real5.2200e+07
I(0) uncertainty (real space) i0_real_error7.8850e+05
Rg (reciprocal space) rg_reciprocal26.43
I(0) (reciprocal space) i0_reciprocal52200000.0000
Solution quality estimate total_estimate0.9003
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.9
Skewness Skewness skewness0.229
Kurtosis Kurtosis kurtosis-0.323
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5772000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.974

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)