6e14

Handover mechanism of the growing pilus by the bacterial outer membrane usher FimD

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Type 1 fimbrin D-mannose specific adhesin

Escherichia coli

UniProt P08191

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 Fimbrial biogenesis outer membrane usher protein × 1 (A0A0F3W955) Protein FimF × 1 (P08189) Protein FimG × 1 (P08190) Chaperone protein FimC × 1 (P31697) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FIMH_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain H; PDBConstruct 1–300; UniProt 1–300

Fimbrial biogenesis outer membrane usher protein

Escherichia coli

UniProt A0A0F3W955

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 Type 1 fimbrin D-mannose specific adhesin × 1 (P08191) Protein FimF × 1 (P08189) Protein FimG × 1 (P08190) Chaperone protein FimC × 1 (P31697) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name A0A0F3W955_ECOLX
Isoform —
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–878; UniProt 1–878

Protein FimF

Escherichia coli

UniProt P08189

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 Type 1 fimbrin D-mannose specific adhesin × 1 (P08191) Fimbrial biogenesis outer membrane usher protein × 1 (A0A0F3W955) Protein FimG × 1 (P08190) Chaperone protein FimC × 1 (P31697) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FIMF_ECOLI
Isoform —
PDB entities 3
Chains and sequence ranges Author chain F; PDBConstruct 2–156; UniProt 22–176

Protein FimG

Escherichia coli

UniProt P08190

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 Type 1 fimbrin D-mannose specific adhesin × 1 (P08191) Fimbrial biogenesis outer membrane usher protein × 1 (A0A0F3W955) Protein FimF × 1 (P08189) Chaperone protein FimC × 1 (P31697) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FIMG_ECOLI
Isoform —
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 2–158; UniProt 11–167

Chaperone protein FimC

Escherichia coli

UniProt P31697

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 Type 1 fimbrin D-mannose specific adhesin × 1 (P08191) Fimbrial biogenesis outer membrane usher protein × 1 (A0A0F3W955) Protein FimF × 1 (P08189) Protein FimG × 1 (P08190) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FIMC_ECOLI
Isoform —
PDB entities 5
Chains and sequence ranges Author chain C; PDBConstruct 1–241; UniProt 1–241

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id6e14
Deposition date deposition_date2018-07-09
Structure title titleHandover mechanism of the growing pilus by the bacterial outer membrane usher FimD
Keywords keywordspili, chaperone, usher, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

6e14__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

6e14__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

6e14__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)46.83 Å
Rg (electron density)48.26 Å
Total Rg48.16 Å
Atom count11991
Residues1586
Excluded volume211230 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 6e14__assembly_1__model_1 pentameric (5) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id6e14C02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6e14G00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id6e14H01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id6e14H02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
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7. Citations (1)