3o0e

Crystal structure of OmpF in complex with colicin peptide OBS1

Method: X-RAY DIFFRACTION Dmax: 128.8 Å Quality: GOOD

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

Porin OmpF

OrganismNot specified

UniProt A0A418U3R0

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 10–349 Chain C; UniProt 10–349 Chain E; UniProt 10–349 Not recorded Colicin-E9 × 3 (P09883) BOG octyl beta-D-glucopyranoside × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;25% PEG 3350, 0.2M Li2SO4, 0.1M sodium cacodylate, pH 6.5, sitting drop vapor diffusion, temperature 293K Resolution 3.01 Å R-free 0.302
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 10–349 Chain D; UniProt 10–349 Chain F; UniProt 10–349 Not recorded Colicin-E9 × 3 (P09883) BOG octyl beta-D-glucopyranoside × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;25% PEG 3350, 0.2M Li2SO4, 0.1M sodium cacodylate, pH 6.5, sitting drop vapor diffusion, temperature 293K Resolution 3.01 Å R-free 0.302

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A418U3R0_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–340; UniProt 10–349 Author chain B; PDBConstruct 1–340; UniProt 10–349 Author chain C; PDBConstruct 1–340; UniProt 10–349 Author chain D; PDBConstruct 1–340; UniProt 10–349 Author chain E; PDBConstruct 1–340; UniProt 10–349 Author chain F; PDBConstruct 1–340; UniProt 10–349

Colicin-E9

OrganismNot specified

UniProt P09883

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 L; UniProt 2–18 Chain N; UniProt 2–18 Chain P; UniProt 2–18 Fragment:UNP Residues 2-18 Porin OmpF × 3 (A0A418U3R0) BOG octyl beta-D-glucopyranoside × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;25% PEG 3350, 0.2M Li2SO4, 0.1M sodium cacodylate, pH 6.5, sitting drop vapor diffusion, temperature 293K Resolution 3.01 Å R-free 0.302
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain M; UniProt 2–18 Chain O; UniProt 2–18 Chain Q; UniProt 2–18 Fragment:UNP Residues 2-18 Porin OmpF × 3 (A0A418U3R0) BOG octyl beta-D-glucopyranoside × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;25% PEG 3350, 0.2M Li2SO4, 0.1M sodium cacodylate, pH 6.5, sitting drop vapor diffusion, temperature 293K Resolution 3.01 Å R-free 0.302

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.

24 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CEA9_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 1–17; UniProt 2–18 Author chain M; PDBConstruct 1–17; UniProt 2–18 Author chain N; PDBConstruct 1–17; UniProt 2–18 Author chain O; PDBConstruct 1–17; UniProt 2–18 Author chain P; PDBConstruct 1–17; UniProt 2–18 Author chain Q; PDBConstruct 1–17; UniProt 2–18

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 3o0e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3o0e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3o0e
Deposition date deposition_date2010-07-19
Structure title titleCrystal structure of OmpF in complex with colicin peptide OBS1
Keywords keywordsporin, membrane protein, complex, colicin; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.92
Radius of gyration Rg (electron density) rg_electron39.99
Forward intensity I(0) i0848898000.00
Molecular weight molecular_weight231880.0 kDa
Excluded volume excluded_volume286110 ų
Envelope volume envelope_volume375350 ų
Hydration-shell volume shell_volume75829 ų
Envelope diameter envelope_diameter135.9
Shell Rg shell_rg47.89
Envelope Rg envelope_rg39.30
Shape Rg shape_rg40.02
Total Rg total_rg40.27
Total atoms total_atoms31693
Residues n_residues2123
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 dmax128.8
Rg (real space) rg_real39.74
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real8.4890e+08
I(0) uncertainty (real space) i0_real_error1.3970e+07
Rg (reciprocal space) rg_reciprocal39.86
I(0) (reciprocal space) i0_reciprocal849000000.0000
Solution quality estimate total_estimate0.8866
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary51.5
Skewness Skewness skewness0.246
Kurtosis Kurtosis kurtosis-0.399
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha288600000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.915

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id3o0eA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology160 — Porin
Homologous superfamily homologous superfamily10 — Porin
Domain ID domain_id3o0eB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology160 — Porin
Homologous superfamily homologous superfamily10 — Porin
Domain ID domain_id3o0eC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology160 — Porin
Homologous superfamily homologous superfamily10 — Porin
Domain ID domain_id3o0eD00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology160 — Porin
Homologous superfamily homologous superfamily10 — Porin
Domain ID domain_id3o0eE00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology160 — Porin
Homologous superfamily homologous superfamily10 — Porin
Domain ID domain_id3o0eF00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology160 — Porin
Homologous superfamily homologous superfamily10 — Porin

8. Citations (1)

9. Files and Curves (10)