4xga

Crystal structure of BamB and BamA P3-5 complex from E.coli

Method: X-RAY DIFFRACTION Dmax: 100.6 Å Quality: GOOD

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

Outer membrane protein assembly factor BamB

Escherichia coli (strain K12)

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 20–392 Not recorded Outer membrane protein assembly factor BamA × 1 (P0A940) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;1% w/v Tryptone, 20% w/v Polyethylene glycol 3350, 0.05M HEPES sodium pH 7.0 Resolution 2.15 Å R-free 0.231

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–373; UniProt 20–392

Outer membrane protein assembly factor BamA

Escherichia coli (strain K12)

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 175–420 Fragment:UNP RESIDUES 175-420 Outer membrane protein assembly factor BamB × 1 (P77774) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;1% w/v Tryptone, 20% w/v Polyethylene glycol 3350, 0.05M HEPES sodium pH 7.0 Resolution 2.15 Å R-free 0.231

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–246; UniProt 175–420

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 4xga

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4xga
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4xga
Deposition date deposition_date2014-12-30
Structure title titleCrystal structure of BamB and BamA P3-5 complex from E.coli
Keywords keywordsouter member protein, PROTEIN BINDING-MEMBRANE PROTEIN complex; PROTEIN BINDING/MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.02
Radius of gyration Rg (electron density) rg_electron27.90
Forward intensity I(0) i053620100.00
Molecular weight molecular_weight56775.0 kDa
Excluded volume excluded_volume70880 ų
Envelope volume envelope_volume89136 ų
Hydration-shell volume shell_volume28437 ų
Envelope diameter envelope_diameter104.7
Shell Rg shell_rg32.78
Envelope Rg envelope_rg28.66
Shape Rg shape_rg27.92
Total Rg total_rg28.33
Total atoms total_atoms4004
Residues n_residues521
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 dmax100.6
Rg (real space) rg_real28.36
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real5.3620e+07
I(0) uncertainty (real space) i0_real_error8.8660e+05
Rg (reciprocal space) rg_reciprocal28.25
I(0) (reciprocal space) i0_reciprocal53620000.0000
Solution quality estimate total_estimate0.8106
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.8
Skewness Skewness skewness0.667
Kurtosis Kurtosis kurtosis0.066
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17700000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.596; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.783; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4xgab1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.391 — POlypeptide TRansport Associated (PORTRA) domain-like
Superfamily Superfamily superfamilyd.391.1 — POlypeptide TRansport Associated (PORTRA) domain-like
Family Family familyd.391.1.0 — automated matches
Domain ID domain_idd4xgab2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.391 — POlypeptide TRansport Associated (PORTRA) domain-like
Superfamily Superfamily superfamilyd.391.1 — POlypeptide TRansport Associated (PORTRA) domain-like
Family Family familyd.391.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id4xgaB01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily310 — membrane protein fhac
Domain ID domain_id4xgaB02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily310 — membrane protein fhac

8. Citations (1)

9. Files and Curves (10)