1qc7

T. MARITIMA FLIG C-TERMINAL DOMAIN

Method: X-RAY DIFFRACTION Dmax: 76.3 Å Quality: GOOD

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

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 235–335 Chain B; UniProt 235–335 Fragment:FLIG-C No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.2;286 K;ISOPROPANOL, pH 5.2, temperature 286K Resolution 2.20 Å R-free 0.304

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–101; UniProt 235–335 Author chain B; PDBConstruct 1–101; UniProt 235–335

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 1qc7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1qc7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1qc7
Deposition date deposition_date1999-05-18
Structure title titleT. MARITIMA FLIG C-TERMINAL DOMAIN
Keywords keywordsFLAGELLAR MOTOR SWITCH PROTEIN, 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_guinier20.47
Radius of gyration Rg (electron density) rg_electron19.72
Forward intensity I(0) i08360340.00
Molecular weight molecular_weight21735.0 kDa
Excluded volume excluded_volume27572 ų
Envelope volume envelope_volume35067 ų
Hydration-shell volume shell_volume15942 ų
Envelope diameter envelope_diameter74.9
Shell Rg shell_rg24.56
Envelope Rg envelope_rg20.33
Shape Rg shape_rg19.68
Total Rg total_rg20.67
Total atoms total_atoms1523
Residues n_residues191
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 dmax76.3
Rg (real space) rg_real20.61
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real8.3600e+06
I(0) uncertainty (real space) i0_real_error1.2580e+05
Rg (reciprocal space) rg_reciprocal20.58
I(0) (reciprocal space) i0_reciprocal8360000.0000
Solution quality estimate total_estimate0.7830
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.7
Skewness Skewness skewness0.622
Kurtosis Kurtosis kurtosis0.221
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3411000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.462; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.808; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1qc7a_
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_idd1qc7b_
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_id1qc7A00
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_id1qc7B00
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)