8pz2

Wait Complex: Lateral open BAM bound Extended SurA

Method: ELECTRON MICROSCOPY Dmax: 143.2 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 21–810 Mutation:R76C 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 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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

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 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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

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 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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

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 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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

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 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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

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 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 43–450; 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 8pz2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8pz2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8pz2
Deposition date deposition_date2023-07-26
最后修订 last_revision2024-09-25
Structure title titleWait Complex: Lateral open BAM bound Extended SurA
Keywords keywordsOuter Membrane, Complex, Chaperone, Protein Folding, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.81
Radius of gyration Rg (electron density) rg_electron45.23
Forward intensity I(0) i0531117000.00
Molecular weight molecular_weight186100.0 kDa
Excluded volume excluded_volume231260 ų
Envelope volume envelope_volume353190 ų
Hydration-shell volume shell_volume65299 ų
Envelope diameter envelope_diameter150.9
Shell Rg shell_rg50.39
Envelope Rg envelope_rg43.58
Shape Rg shape_rg45.24
Total Rg total_rg45.45
Total atoms total_atoms13121
Residues n_residues1678
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 dmax143.2
Rg (real space) rg_real45.64
Rg uncertainty (real space) rg_real_error1.02
I(0) (real space) i0_real5.3110e+08
I(0) uncertainty (real space) i0_real_error9.6950e+06
Rg (reciprocal space) rg_reciprocal45.80
I(0) (reciprocal space) i0_reciprocal531200000.0000
Solution quality estimate total_estimate0.8888
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.2
Skewness Skewness skewness0.110
Kurtosis Kurtosis kurtosis-0.568
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha54510000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.722

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)