9h84

BAM-hinge (LVPR)

Method: ELECTRON MICROSCOPY Dmax: 133.4 Å Quality: GOOD

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

Outer membrane protein assembly factor BamA

Escherichia coli

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 92–810 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 (P0AC04) Outer membrane protein assembly factor BamE × 1 (P0A938) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 1–723; UniProt 92–810

Outer membrane protein assembly factor BamB

Escherichia coli

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 22–392 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 (P0AC04) Outer membrane protein assembly factor BamE × 1 (P0A938) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 1–371; UniProt 22–392

Outer membrane protein assembly factor BamC

Escherichia coli

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 25–91 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 (P0AC04) Outer membrane protein assembly factor BamE × 1 (P0A938) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 1–67; UniProt 25–91

Outer membrane protein assembly factor BamD

Escherichia coli

UniProt P0AC04

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 26–243 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 (P0A938) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 BAMD_ECO57
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–218; UniProt 26–243

Outer membrane protein assembly factor BamE

Escherichia coli

UniProt P0A938

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 23–113 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 (P0AC04) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 BAME_ECOL6
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–91; UniProt 23–113

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 9h84

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9h84
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9h84
Deposition date deposition_date2024-10-28
最后修订 last_revision2025-10-22
Structure title titleBAM-hinge (LVPR)
Keywords keywordsOuter membrane, folding, OMP, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.58
Radius of gyration Rg (electron density) rg_electron42.16
Forward intensity I(0) i0408125000.00
Molecular weight molecular_weight162700.0 kDa
Excluded volume excluded_volume202290 ų
Envelope volume envelope_volume282040 ų
Hydration-shell volume shell_volume56601 ų
Envelope diameter envelope_diameter133.7
Shell Rg shell_rg46.77
Envelope Rg envelope_rg40.72
Shape Rg shape_rg42.16
Total Rg total_rg42.41
Total atoms total_atoms22540
Residues n_residues1466
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 dmax133.4
Rg (real space) rg_real42.47
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real4.0810e+08
I(0) uncertainty (real space) i0_real_error6.6450e+06
Rg (reciprocal space) rg_reciprocal42.58
I(0) (reciprocal space) i0_reciprocal408200000.0000
Solution quality estimate total_estimate0.8951
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.3
Skewness Skewness skewness0.103
Kurtosis Kurtosis kurtosis-0.726
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha50790000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.776

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)