8ya2

Structure of the SecA-SecY complex with the substrate FtsQ-LacY(+20C)

Method: ELECTRON MICROSCOPY Dmax: 134.2 Å Quality: GOOD

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 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–778 Not recorded Protein translocase subunit SecY × 1 (A4IJK8) Protein translocase subunit SecE × 1 (A4IJH4) Cell division protein FtsQ,Lactose permease × 1 (P06136,P02920) Nanobody × 1 Green fluorescent protein × 1 (P42212) 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 3.84 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 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) 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) Cell division protein FtsQ,Lactose permease × 1 (P06136,P02920) Nanobody × 1 Green fluorescent protein × 1 (P42212) 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 3.84 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 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 1–60 Not recorded Protein translocase subunit SecA × 1 (P28366) Protein translocase subunit SecY × 1 (A4IJK8) Cell division protein FtsQ,Lactose permease × 1 (P06136,P02920) Nanobody × 1 Green fluorescent protein × 1 (P42212) 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 3.84 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

Cell division protein FtsQ,Lactose permease

Escherichia coli K-12

UniProt P02920

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 315–334 Mutation:T1M,R2A,L3K,A4K,G5T,E45C,C53A Protein translocase subunit SecA × 1 (P28366) Protein translocase subunit SecY × 1 (A4IJK8) Protein translocase subunit SecE × 1 (A4IJH4) Nanobody × 1 Green fluorescent protein × 1 (P42212) 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 3.84 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 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LACY_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 35–54; UniProt 315–334

Cell division protein FtsQ,Lactose permease

Escherichia coli K-12

UniProt P06136

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 23–47 Mutation:T1M,R2A,L3K,A4K,G5T,E45C,C53A Protein translocase subunit SecA × 1 (P28366) Protein translocase subunit SecY × 1 (A4IJK8) Protein translocase subunit SecE × 1 (A4IJH4) Nanobody × 1 Green fluorescent protein × 1 (P42212) 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 3.84 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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FTSQ_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–25; UniProt 23–47

Green fluorescent protein

Aequorea victoria

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 3–229 Mutation:Q80R, F99S, M153T, V163A Non-standard monomer:Yes (specific site not provided by mmCIF) Protein translocase subunit SecA × 1 (P28366) Protein translocase subunit SecY × 1 (A4IJK8) Protein translocase subunit SecE × 1 (A4IJH4) Cell division protein FtsQ,Lactose permease × 1 (P06136,P02920) Nanobody × 1 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 3.84 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 6
Chains and sequence ranges Author chain G; PDBConstruct 1–225; UniProt 3–229

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 8ya2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ya2
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8ya2
Deposition date deposition_date2024-02-07
Structure title titleStructure of the SecA-SecY complex with the substrate FtsQ-LacY(+20C)
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_guinier41.59
Radius of gyration Rg (electron density) rg_electron41.41
Forward intensity I(0) i0481038000.00
Molecular weight molecular_weight183230.0 kDa
Excluded volume excluded_volume231140 ų
Envelope volume envelope_volume321930 ų
Hydration-shell volume shell_volume65330 ų
Envelope diameter envelope_diameter140.8
Shell Rg shell_rg46.23
Envelope Rg envelope_rg40.76
Shape Rg shape_rg41.42
Total Rg total_rg41.64
Total atoms total_atoms12899
Residues n_residues1620
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 dmax134.2
Rg (real space) rg_real41.50
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real4.8100e+08
I(0) uncertainty (real space) i0_real_error9.1490e+06
Rg (reciprocal space) rg_reciprocal41.59
I(0) (reciprocal space) i0_reciprocal481100000.0000
Solution quality estimate total_estimate0.8973
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.4
Skewness Skewness skewness0.215
Kurtosis Kurtosis kurtosis-0.522
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha59400000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.933; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.865

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)