3k1b

Structure of OmpF porin

Method: X-RAY DIFFRACTION Dmax: 132.2 Å Quality: GOOD

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

Outer membrane protein F

OrganismNot specified

UniProt P02931

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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 23–362 Chain B; UniProt 23–362 Chain C; UniProt 23–362 Fragment:sequence database residues 1-340 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 3.9;293 K;0.48 sodium phosphate monobasic, 0.72 M potassium phosphate monobasic, 0.1 M acetate pH 3.9, VAPOR DIFFUSION, temperature 293K Resolution 4.39 Å R-free 0.329
2 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 23–362 Fragment:sequence database residues 1-340 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 3.9;293 K;0.48 sodium phosphate monobasic, 0.72 M potassium phosphate monobasic, 0.1 M acetate pH 3.9, VAPOR DIFFUSION, temperature 293K Resolution 4.39 Å R-free 0.329

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.

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

View Construct and Data Evidence
UniProt name OMPF_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–340; UniProt 23–362 Author chain B; PDBConstruct 1–340; UniProt 23–362 Author chain C; PDBConstruct 1–340; UniProt 23–362 Author chain D; PDBConstruct 1–340; UniProt 23–362

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 3k1b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3k1b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3k1b
Deposition date deposition_date2009-09-26
Structure title titleStructure of OmpF porin
Keywords keywords;OmpF porin, FOSCHOLINE-12, Structural Genomics, PSI-2, Protein Structure Initiative, Center for Structures of Membrane Proteins, CSMP, Cell membrane, Cell outer membrane, Ion transport, Membrane, Phage recognition, Porin, Transmembrane, Transport, TRANSPORT PROTEIN, MEMBRANE PROTEIN ;; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.75
Radius of gyration Rg (electron density) rg_electron39.16
Forward intensity I(0) i0350944000.00
Molecular weight molecular_weight148290.0 kDa
Excluded volume excluded_volume183340 ų
Envelope volume envelope_volume248010 ų
Hydration-shell volume shell_volume53712 ų
Envelope diameter envelope_diameter140.3
Shell Rg shell_rg43.94
Envelope Rg envelope_rg38.77
Shape Rg shape_rg39.18
Total Rg total_rg39.36
Total atoms total_atoms10508
Residues n_residues1360
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 dmax132.2
Rg (real space) rg_real38.87
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real3.5090e+08
I(0) uncertainty (real space) i0_real_error6.7830e+06
Rg (reciprocal space) rg_reciprocal38.80
I(0) (reciprocal space) i0_reciprocal350900000.0000
Solution quality estimate total_estimate0.8666
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.7
Skewness Skewness skewness0.418
Kurtosis Kurtosis kurtosis-0.290
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha75660000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.807; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.860

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)