1mpf

STRUCTURAL AND FUNCTIONAL ALTERATIONS OF A COLICIN RESISTANT MUTANT OF OMPF-PORIN FROM ESCHERICHIA COLI

Method: X-RAY DIFFRACTION Dmax: 69.9 Å Quality: REASONABLE

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

MATRIX PORIN OUTER MEMBRANE PROTEIN F

Escherichia coli

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 Not recorded C8E (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE × 36 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 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 1–340; 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 1mpf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1mpf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1mpf
Deposition date deposition_date1994-08-10
Structure title titleSTRUCTURAL AND FUNCTIONAL ALTERATIONS OF A COLICIN RESISTANT MUTANT OF OMPF-PORIN FROM ESCHERICHIA COLI
Keywords keywordsMEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.52
Radius of gyration Rg (electron density) rg_electron20.82
Forward intensity I(0) i024509600.00
Molecular weight molecular_weight38152.0 kDa
Excluded volume excluded_volume47787 ų
Envelope volume envelope_volume58535 ų
Hydration-shell volume shell_volume23192 ų
Envelope diameter envelope_diameter70.3
Shell Rg shell_rg27.89
Envelope Rg envelope_rg20.84
Shape Rg shape_rg20.81
Total Rg total_rg21.78
Total atoms total_atoms2703
Residues n_residues340
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 dmax69.9
Rg (real space) rg_real21.38
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real2.4510e+07
I(0) uncertainty (real space) i0_real_error3.4530e+05
Rg (reciprocal space) rg_reciprocal21.41
I(0) (reciprocal space) i0_reciprocal24510000.0000
Solution quality estimate total_estimate0.6833
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.8
Skewness Skewness skewness0.139
Kurtosis Kurtosis kurtosis-0.301
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2724000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.801; Stabil: 1.000; Sysdev: 0.161; Positv: 1.000; Valcen: 0.997; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1mpfa_
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

CATH v4.4 (1 domains)

Domain ID domain_id1mpfA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology160 — Porin
Homologous superfamily homologous superfamily10 — Porin

8. Citations (2)

9. Files and Curves (10)