6wtz

Cryo-EM structure of E. Coli OmpF

Method: ELECTRON MICROSCOPY Dmax: 90.7 Å Quality: EXCELLENT

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

Outer membrane porin 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 1–362 Chain B; UniProt 1–362 Chain C; UniProt 1–362 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.15 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.

41 other PDB entries and 64 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 1–362; UniProt 1–362 Author chain B; PDBConstruct 1–362; UniProt 1–362 Author chain C; PDBConstruct 1–362; UniProt 1–362

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 6wtz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6wtz
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6wtz
Deposition date deposition_date2020-05-04
Structure title titleCryo-EM structure of E. Coli OmpF
Keywords keywordsouter membrane porin, omp, ompf, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.27
Radius of gyration Rg (electron density) rg_electron30.71
Forward intensity I(0) i0206960000.00
Molecular weight molecular_weight111220.0 kDa
Excluded volume excluded_volume137500 ų
Envelope volume envelope_volume183810 ų
Hydration-shell volume shell_volume47948 ų
Envelope diameter envelope_diameter93.5
Shell Rg shell_rg39.49
Envelope Rg envelope_rg30.36
Shape Rg shape_rg30.71
Total Rg total_rg31.49
Total atoms total_atoms7881
Residues n_residues1020
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 dmax90.7
Rg (real space) rg_real31.03
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real2.0700e+08
I(0) uncertainty (real space) i0_real_error2.6580e+06
Rg (reciprocal space) rg_reciprocal31.14
I(0) (reciprocal space) i0_reciprocal207000000.0000
Solution quality estimate total_estimate0.9087
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.3
Skewness Skewness skewness0.050
Kurtosis Kurtosis kurtosis-0.634
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19010000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.971; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.919

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd6wtza_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.4 — Transmembrane beta-barrels
Superfamily Superfamily superfamilyf.4.3 — Porins
Family Family familyf.4.3.1 — Porin
Domain ID domain_idd6wtzb_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.4 — Transmembrane beta-barrels
Superfamily Superfamily superfamilyf.4.3 — Porins
Family Family familyf.4.3.1 — Porin
Domain ID domain_idd6wtzc_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.4 — Transmembrane beta-barrels
Superfamily Superfamily superfamilyf.4.3 — Porins
Family Family familyf.4.3.1 — Porin

8. Citations (1)

9. Files and Curves (10)