9hg7

BAM-SurA complex in the swing-out state

Method: ELECTRON MICROSCOPY Dmax: 159.8 Å Quality: GOOD

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

Outer membrane protein assembly factor BamA

Escherichia coli K-12

UniProt P0A940

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 A; UniProt 21–810 Not recorded Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamC × 1 (P0A903) Outer membrane protein assembly factor BamD × 1 (P0AC02) Outer membrane protein assembly factor BamE × 1 (P0A937) Chaperone SurA × 1 (P0ABZ6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20mM Tris-HCl, 150mM NaCl, 0.05% DDM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.83 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.

64 other PDB entries and 69 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAMA_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–790; UniProt 21–810

Outer membrane protein assembly factor BamB

Escherichia coli K-12

UniProt P77774

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 B; UniProt 20–392 Not recorded Outer membrane protein assembly factor BamA × 1 (P0A940) Outer membrane protein assembly factor BamC × 1 (P0A903) Outer membrane protein assembly factor BamD × 1 (P0AC02) Outer membrane protein assembly factor BamE × 1 (P0A937) Chaperone SurA × 1 (P0ABZ6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20mM Tris-HCl, 150mM NaCl, 0.05% DDM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.83 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.

63 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAMB_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–373; UniProt 20–392

Outer membrane protein assembly factor BamC

Escherichia coli K-12

UniProt P0A903

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 25–344 Not recorded Outer membrane protein assembly factor BamA × 1 (P0A940) Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamD × 1 (P0AC02) Outer membrane protein assembly factor BamE × 1 (P0A937) Chaperone SurA × 1 (P0ABZ6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20mM Tris-HCl, 150mM NaCl, 0.05% DDM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.83 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.

51 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAMC_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–320; UniProt 25–344

Outer membrane protein assembly factor BamD

Escherichia coli K-12

UniProt P0AC02

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 20–245 Not recorded Outer membrane protein assembly factor BamA × 1 (P0A940) Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamC × 1 (P0A903) Outer membrane protein assembly factor BamE × 1 (P0A937) Chaperone SurA × 1 (P0ABZ6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20mM Tris-HCl, 150mM NaCl, 0.05% DDM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.83 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.

46 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAMD_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–226; UniProt 20–245

Outer membrane protein assembly factor BamE

Escherichia coli K-12

UniProt P0A937

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 20–113 Not recorded Outer membrane protein assembly factor BamA × 1 (P0A940) Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamC × 1 (P0A903) Outer membrane protein assembly factor BamD × 1 (P0AC02) Chaperone SurA × 1 (P0ABZ6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20mM Tris-HCl, 150mM NaCl, 0.05% DDM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.83 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.

46 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAME_ECOLI
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–94; UniProt 20–113

Chaperone SurA

Escherichia coli K-12

UniProt P0ABZ6

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 21–428 Not recorded Outer membrane protein assembly factor BamA × 1 (P0A940) Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamC × 1 (P0A903) Outer membrane protein assembly factor BamD × 1 (P0AC02) Outer membrane protein assembly factor BamE × 1 (P0A937) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20mM Tris-HCl, 150mM NaCl, 0.05% DDM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.83 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.

17 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SURA_ECOLI
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 5–412; UniProt 21–428

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 9hg7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9hg7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9hg7
Deposition date deposition_date2024-11-19
最后修订 last_revision2025-04-16
Structure title titleBAM-SurA complex in the swing-out state
Keywords keywordsinsertase, outer membrane protein, chaperone, protein folding, protein complex, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.16
Radius of gyration Rg (electron density) rg_electron48.52
Forward intensity I(0) i0709373000.00
Molecular weight molecular_weight216130.0 kDa
Excluded volume excluded_volume268360 ų
Envelope volume envelope_volume404320 ų
Hydration-shell volume shell_volume69142 ų
Envelope diameter envelope_diameter162.0
Shell Rg shell_rg53.58
Envelope Rg envelope_rg46.95
Shape Rg shape_rg48.52
Total Rg total_rg48.70
Total atoms total_atoms30038
Residues n_residues1953
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 dmax159.8
Rg (real space) rg_real49.00
Rg uncertainty (real space) rg_real_error1.37
I(0) (real space) i0_real7.0940e+08
I(0) uncertainty (real space) i0_real_error1.2840e+07
Rg (reciprocal space) rg_reciprocal49.16
I(0) (reciprocal space) i0_reciprocal709500000.0000
Solution quality estimate total_estimate0.8798
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.9
Skewness Skewness skewness0.125
Kurtosis Kurtosis kurtosis-0.548
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57600000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.747

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)