2wwb

CRYO-EM STRUCTURE OF THE MAMMALIAN SEC61 COMPLEX BOUND TO THE ACTIVELY TRANSLATING WHEAT GERM 80S RIBOSOME

Method: ELECTRON MICROSCOPY Dmax: 154.9 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–RNA Heteromer Protein × 11 RNA 4 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain A; UniProt 1–476 Not recorded PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT GAMMA × 1 (P60058) PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT BETA × 1 (P60467) 5.8S RRNA × 1 25S RRNA × 1 25S RRNA × 1 25S RRNA × 1 60S RIBOSOMAL PROTEIN L4-B × 1 60S RIBOSOMAL PROTEIN L17-A × 1 60S RIBOSOMAL PROTEIN L19 × 1 60S RIBOSOMAL PROTEIN L25 × 1 60S RIBOSOMAL PROTEIN L26-A × 1 60S RIBOSOMAL PROTEIN L31-A × 1 60S RIBOSOMAL PROTEIN L35 × 1 60S RIBOSOMAL PROTEIN L39 × 1 ELECTRON MICROSCOPY cryo-EM buffer:30 MM HEPES/KOH, PH 7.5 180 MM KOAC, 10 MM MG(OAC)2, 1 MM DTT, 3.5 % (W/V) GLYCEROL 0.3 % (W/V) DIGITONIN;pH 7.5;30 MM HEPES/KOH, PH 7.5 180 MM KOAC, 10 MM MG(OAC)2, 1 MM DTT, 3.5 % (W/V) GLYCEROL 0.3 % (W/V) DIGITONIN cryo-EM vitrification conditions:Cryogen ETHANE;CRYOGEN- ETHANE, HUMIDITY- 95, INSTRUMENT- VITROBOT, METHOD- BLOT FOR 10 SECONDS BEFORE PLUNGING, USE 2 LAYERS OF FILTER PAPER Resolution 6.48 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–RNA Heteromer Protein × 11 RNA 4 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain B; UniProt 1–68 Not recorded PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT ALPHA ISOFORM 1 × 1 (P38377) PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT BETA × 1 (P60467) 5.8S RRNA × 1 25S RRNA × 1 25S RRNA × 1 25S RRNA × 1 60S RIBOSOMAL PROTEIN L4-B × 1 60S RIBOSOMAL PROTEIN L17-A × 1 60S RIBOSOMAL PROTEIN L19 × 1 60S RIBOSOMAL PROTEIN L25 × 1 60S RIBOSOMAL PROTEIN L26-A × 1 60S RIBOSOMAL PROTEIN L31-A × 1 60S RIBOSOMAL PROTEIN L35 × 1 60S RIBOSOMAL PROTEIN L39 × 1 ELECTRON MICROSCOPY cryo-EM buffer:30 MM HEPES/KOH, PH 7.5 180 MM KOAC, 10 MM MG(OAC)2, 1 MM DTT, 3.5 % (W/V) GLYCEROL 0.3 % (W/V) DIGITONIN;pH 7.5;30 MM HEPES/KOH, PH 7.5 180 MM KOAC, 10 MM MG(OAC)2, 1 MM DTT, 3.5 % (W/V) GLYCEROL 0.3 % (W/V) DIGITONIN cryo-EM vitrification conditions:Cryogen ETHANE;CRYOGEN- ETHANE, HUMIDITY- 95, INSTRUMENT- VITROBOT, METHOD- BLOT FOR 10 SECONDS BEFORE PLUNGING, USE 2 LAYERS OF FILTER PAPER Resolution 6.48 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

PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT BETA

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–RNA Heteromer Protein × 11 RNA 4 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain C; UniProt 1–96 Not recorded PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT ALPHA ISOFORM 1 × 1 (P38377) PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT GAMMA × 1 (P60058) 5.8S RRNA × 1 25S RRNA × 1 25S RRNA × 1 25S RRNA × 1 60S RIBOSOMAL PROTEIN L4-B × 1 60S RIBOSOMAL PROTEIN L17-A × 1 60S RIBOSOMAL PROTEIN L19 × 1 60S RIBOSOMAL PROTEIN L25 × 1 60S RIBOSOMAL PROTEIN L26-A × 1 60S RIBOSOMAL PROTEIN L31-A × 1 60S RIBOSOMAL PROTEIN L35 × 1 60S RIBOSOMAL PROTEIN L39 × 1 ELECTRON MICROSCOPY cryo-EM buffer:30 MM HEPES/KOH, PH 7.5 180 MM KOAC, 10 MM MG(OAC)2, 1 MM DTT, 3.5 % (W/V) GLYCEROL 0.3 % (W/V) DIGITONIN;pH 7.5;30 MM HEPES/KOH, PH 7.5 180 MM KOAC, 10 MM MG(OAC)2, 1 MM DTT, 3.5 % (W/V) GLYCEROL 0.3 % (W/V) DIGITONIN cryo-EM vitrification conditions:Cryogen ETHANE;CRYOGEN- ETHANE, HUMIDITY- 95, INSTRUMENT- VITROBOT, METHOD- BLOT FOR 10 SECONDS BEFORE PLUNGING, USE 2 LAYERS OF FILTER PAPER Resolution 6.48 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–96; UniProt 1–96

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 2wwb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2wwb
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2wwb
Deposition date deposition_date2009-10-22
Structure title titleCRYO-EM STRUCTURE OF THE MAMMALIAN SEC61 COMPLEX BOUND TO THE ACTIVELY TRANSLATING WHEAT GERM 80S RIBOSOME
Keywords keywordsRIBOSOME, PROTEIN EXIT TUNNEL, COTRANSLATIONAL PROTEIN TRANSLOCATION, PROTEIN CONDUCTING CHANNEL, SIGNAL SEQUENCE; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.94
Radius of gyration Rg (electron density) rg_electron46.58
Forward intensity I(0) i0804995000.00
Molecular weight molecular_weight206110.0 kDa
Excluded volume excluded_volume247010 ų
Envelope volume envelope_volume407280 ų
Hydration-shell volume shell_volume74704 ų
Envelope diameter envelope_diameter170.2
Shell Rg shell_rg49.46
Envelope Rg envelope_rg45.81
Shape Rg shape_rg46.66
Total Rg total_rg46.48
Total atoms total_atoms14313
Residues n_residues1591
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 dmax154.9
Rg (real space) rg_real44.99
Rg uncertainty (real space) rg_real_error1.31
I(0) (real space) i0_real8.0500e+08
I(0) uncertainty (real space) i0_real_error1.3130e+07
Rg (reciprocal space) rg_reciprocal44.94
I(0) (reciprocal space) i0_reciprocal804900000.0000
Solution quality estimate total_estimate0.8555
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.5
Skewness Skewness skewness0.428
Kurtosis Kurtosis kurtosis0.013
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha49810000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.783; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.773

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

8. Citations (1)

9. Files and Curves (10)