8yas

Structure of the SecA-SecY complex with the substrate HmBRI-7TM

Method: ELECTRON MICROSCOPY Dmax: 113.2 Å Quality: EXCELLENT

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

Protein translocase subunit SecA

Bacillus subtilis subsp. subtilis str. 168

UniProt P28366

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 1–778 Not recorded Protein translocase subunit SecY × 1 (A4IJK8) Protein translocase subunit SecE × 1 (A4IJH4) MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.97 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.

16 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SECA_BACSU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–778; UniProt 1–778

Protein translocase subunit SecY

Geobacillus thermodenitrificans NG80-2

UniProt A4IJK8

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 Y; UniProt 1–430 Mutation:G60C, Q202T, F211T, R213N Protein translocase subunit SecA × 1 (P28366) Protein translocase subunit SecE × 1 (A4IJH4) MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.97 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A4IJK8_GEOTN
Isoform
PDB entities 2
Chains and sequence ranges Author chain Y; PDBConstruct 1–430; UniProt 1–430

Protein translocase subunit SecE

Geobacillus thermodenitrificans NG80-2

UniProt A4IJH4

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 E; UniProt 1–60 Not recorded Protein translocase subunit SecA × 1 (P28366) Protein translocase subunit SecY × 1 (A4IJK8) MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.97 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A4IJH4_GEOTN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–60; UniProt 1–60

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 8yas

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8yas
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8yas
Deposition date deposition_date2024-02-10
Structure title titleStructure of the SecA-SecY complex with the substrate HmBRI-7TM
Keywords keywordsProtein translocation, SecY, Membrane protein insertion, Protein chaperone, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.91
Radius of gyration Rg (electron density) rg_electron36.57
Forward intensity I(0) i0286372000.00
Molecular weight molecular_weight140630.0 kDa
Excluded volume excluded_volume177820 ų
Envelope volume envelope_volume236550 ų
Hydration-shell volume shell_volume53613 ų
Envelope diameter envelope_diameter121.8
Shell Rg shell_rg43.03
Envelope Rg envelope_rg36.04
Shape Rg shape_rg36.57
Total Rg total_rg36.98
Total atoms total_atoms9894
Residues n_residues1243
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 dmax113.2
Rg (real space) rg_real36.78
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real2.8640e+08
I(0) uncertainty (real space) i0_real_error4.4270e+06
Rg (reciprocal space) rg_reciprocal36.86
I(0) (reciprocal space) i0_reciprocal286400000.0000
Solution quality estimate total_estimate0.9025
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.1
Skewness Skewness skewness0.182
Kurtosis Kurtosis kurtosis-0.598
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41380000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.972; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.815

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)