1lkv

Crystal Structure of the Middle and C-terminal Domains of the Flagellar Rotor Protein FliG

Method: X-RAY DIFFRACTION Dmax: 88.8 Å Quality: REASONABLE

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

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
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain X; UniProt 104–335 Fragment:RESIDUES 104-335 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.5;298 K;Isopropanol, CaCl2, sodium acetate, pluronic F-68, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.80 Å R-free 0.280
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain X; UniProt 104–335 Fragment:RESIDUES 104-335 CA CALCIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.5;298 K;Isopropanol, CaCl2, sodium acetate, pluronic F-68, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.80 Å R-free 0.280

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 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIG_THEMA
Isoform
PDB entities 1
Chains and sequence ranges Author chain X; PDBConstruct 1–232; UniProt 104–335

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 1lkv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1lkv
Deposition date deposition_date2002-04-25
Structure title titleCrystal Structure of the Middle and C-terminal Domains of the Flagellar Rotor Protein FliG
Keywords keywordschemotaxis, flagella, flagellar motion, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.93
Radius of gyration Rg (electron density) rg_electron27.55
Forward intensity I(0) i09782250.00
Molecular weight molecular_weight24301.0 kDa
Excluded volume excluded_volume30783 ų
Envelope volume envelope_volume46611 ų
Hydration-shell volume shell_volume15330 ų
Envelope diameter envelope_diameter85.5
Shell Rg shell_rg32.26
Envelope Rg envelope_rg26.30
Shape Rg shape_rg27.56
Total Rg total_rg28.16
Total atoms total_atoms1703
Residues n_residues213
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 dmax88.8
Rg (real space) rg_real28.15
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real9.7820e+06
I(0) uncertainty (real space) i0_real_error1.6210e+05
Rg (reciprocal space) rg_reciprocal28.09
I(0) (reciprocal space) i0_reciprocal9782000.0000
Solution quality estimate total_estimate0.5592
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.2
Skewness Skewness skewness0.253
Kurtosis Kurtosis kurtosis-0.996
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha748900.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.738; Stabil: 1.000; Sysdev: 0.177; Positv: 1.000; Valcen: 0.521; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1lkvx_
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

CATH v4.4 (2 domains)

Domain ID domain_id1lkvX01
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_id1lkvX02
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)