5mg3

EM fitted model of bacterial holo-translocon

Method: ELECTRON MICROSCOPY Dmax: 124.1 Å Quality: GOOD

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

Protein translocase subunit SecY

Escherichia coli

UniProt P0AGA2

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain Y; UniProt 1–443 Not recorded Protein translocase subunit SecE × 1 (P0AG96) Protein-export membrane protein SecG × 1 (P0AG99) Protein translocase subunit SecD × 1 (P0AG90) Protein translocase subunit SecF × 1 (P0AG93) Membrane protein insertase YidC × 1 (P25714) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 14.00 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SECY_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain Y; PDBConstruct 16–458; UniProt 1–443

Protein translocase subunit SecE

Escherichia coli

UniProt P0AG96

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 3–127 Not recorded Protein translocase subunit SecY × 1 (P0AGA2) Protein-export membrane protein SecG × 1 (P0AG99) Protein translocase subunit SecD × 1 (P0AG90) Protein translocase subunit SecF × 1 (P0AG93) Membrane protein insertase YidC × 1 (P25714) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 14.00 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SECE_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 16–140; UniProt 3–127

Protein-export membrane protein SecG

Escherichia coli

UniProt P0AG99

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 1–110 Not recorded Protein translocase subunit SecY × 1 (P0AGA2) Protein translocase subunit SecE × 1 (P0AG96) Protein translocase subunit SecD × 1 (P0AG90) Protein translocase subunit SecF × 1 (P0AG93) Membrane protein insertase YidC × 1 (P25714) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 14.00 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SECG_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 27–136; UniProt 1–110

Protein translocase subunit SecD

Escherichia coli

UniProt P0AG90

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 2–615 Not recorded Protein translocase subunit SecY × 1 (P0AGA2) Protein translocase subunit SecE × 1 (P0AG96) Protein-export membrane protein SecG × 1 (P0AG99) Protein translocase subunit SecF × 1 (P0AG93) Membrane protein insertase YidC × 1 (P25714) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 14.00 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.

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

View Construct and Data Evidence
UniProt name SECD_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 9–622; UniProt 2–615

Protein translocase subunit SecF

Escherichia coli

UniProt P0AG93

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain F; UniProt 1–323 Not recorded Protein translocase subunit SecY × 1 (P0AGA2) Protein translocase subunit SecE × 1 (P0AG96) Protein-export membrane protein SecG × 1 (P0AG99) Protein translocase subunit SecD × 1 (P0AG90) Membrane protein insertase YidC × 1 (P25714) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 14.00 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.

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

View Construct and Data Evidence
UniProt name SECF_ECOLI
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 1–323; UniProt 1–323

Membrane protein insertase YidC

Escherichia coli

UniProt P25714

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 2–548 Not recorded Protein translocase subunit SecY × 1 (P0AGA2) Protein translocase subunit SecE × 1 (P0AG96) Protein-export membrane protein SecG × 1 (P0AG99) Protein translocase subunit SecD × 1 (P0AG90) Protein translocase subunit SecF × 1 (P0AG93) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 14.00 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.

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

View Construct and Data Evidence
UniProt name YIDC_ECOLI
Isoform
PDB entities 6
Chains and sequence ranges Author chain C; PDBConstruct 7–553; UniProt 2–548

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 5mg3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5mg3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5mg3
Deposition date deposition_date2016-11-20
Structure title titleEM fitted model of bacterial holo-translocon
Keywords keywordsholotranslocon, membrane protein insertion machinery, chaperone, protein secretion; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.04
Radius of gyration Rg (electron density) rg_electron38.07
Forward intensity I(0) i0459057000.00
Molecular weight molecular_weight185980.0 kDa
Excluded volume excluded_volume237980 ų
Envelope volume envelope_volume322940 ų
Hydration-shell volume shell_volume68529 ų
Envelope diameter envelope_diameter131.4
Shell Rg shell_rg45.61
Envelope Rg envelope_rg37.72
Shape Rg shape_rg38.08
Total Rg total_rg38.55
Total atoms total_atoms26650
Residues n_residues1698
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 dmax124.1
Rg (real space) rg_real38.83
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real4.5910e+08
I(0) uncertainty (real space) i0_real_error8.1880e+06
Rg (reciprocal space) rg_reciprocal38.97
I(0) (reciprocal space) i0_reciprocal459100000.0000
Solution quality estimate total_estimate0.8964
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.6
Skewness Skewness skewness0.177
Kurtosis Kurtosis kurtosis-0.466
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76980000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.916; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.911

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)