4fhr

Crystal structure of the complex between the flagellar motor proteins FliG and FliM.

Method: X-RAY DIFFRACTION Dmax: 107.0 Å Quality: REASONABLE

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

Flagellar motor switch protein FliM

Thermotoga maritima

UniProt Q9WZE6

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 46–230 Fragment:Middle domain, UNP residues 46-230 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;50 mM calcium acetate, 0.1 M sodium cacodylate pH 6.0, and 25% v/v MPD, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.93 Å R-free 0.243

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.

4 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9WZE6_THEMA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–187; UniProt 46–230

Flagellar motor switch protein FliG

Thermotoga maritima

UniProt Q9WY63

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 115–327 Fragment:Middle and C-terminal domains. UNP residues 115-327 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;50 mM calcium acetate, 0.1 M sodium cacodylate pH 6.0, and 25% v/v MPD, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.93 Å R-free 0.243

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.

6 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIG_THEMA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–216; UniProt 115–327

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 4fhr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4fhr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4fhr
Deposition date deposition_date2012-06-06
Structure title titleCrystal structure of the complex between the flagellar motor proteins FliG and FliM.
Keywords keywordsflagellar motor, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.95
Radius of gyration Rg (electron density) rg_electron30.20
Forward intensity I(0) i030447900.00
Molecular weight molecular_weight44602.0 kDa
Excluded volume excluded_volume56607 ų
Envelope volume envelope_volume72555 ų
Hydration-shell volume shell_volume22736 ų
Envelope diameter envelope_diameter111.6
Shell Rg shell_rg32.84
Envelope Rg envelope_rg30.81
Shape Rg shape_rg30.21
Total Rg total_rg30.45
Total atoms total_atoms3138
Residues n_residues390
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 dmax107.0
Rg (real space) rg_real30.44
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real3.0450e+07
I(0) uncertainty (real space) i0_real_error5.0860e+05
Rg (reciprocal space) rg_reciprocal30.23
I(0) (reciprocal space) i0_reciprocal30440000.0000
Solution quality estimate total_estimate0.7343
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.662
Kurtosis Kurtosis kurtosis-0.222
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14040000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.481; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.335; Smooth: 0.765

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4fhrb1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.14 — FliG
Family Family familya.118.14.1 — FliG
Domain ID domain_idd4fhrb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (3 domains)

Domain ID domain_id4fhrA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1550 — Chemotaxis protein chec
Homologous superfamily homologous superfamily10 — CheC-like
Domain ID domain_id4fhrB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily30 — Flagellar motor switch protein FliG, alpha-alpha superhelical domain
Domain ID domain_id4fhrB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily30 — Flagellar motor switch protein FliG, alpha-alpha superhelical domain

8. Citations (1)

9. Files and Curves (10)