8s8r

An induced-fit motion of a mobile loop

Method: X-RAY DIFFRACTION Dmax: 57.7 Å Quality: GOOD

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

Imidazole glycerol phosphate synthase subunit HisF

Thermotoga maritima

UniProt Q9X0C6

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 D; UniProt 1–253 Not recorded PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;277 K;ammonium phosphate Resolution 1.20 Å R-free 0.208

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.

24 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HIS6_THEMA
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 1–253; UniProt 1–253

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 8s8r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8s8r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8s8r
Deposition date deposition_date2024-03-07
最后修订 last_revision2025-02-19
Structure title titleAn induced-fit motion of a mobile loop
Keywords keywordsimidazole glycerol phosphate synthase, 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_guinier18.61
Radius of gyration Rg (electron density) rg_electron17.39
Forward intensity I(0) i013429400.00
Molecular weight molecular_weight27794.0 kDa
Excluded volume excluded_volume34971 ų
Envelope volume envelope_volume39346 ų
Hydration-shell volume shell_volume18580 ų
Envelope diameter envelope_diameter59.4
Shell Rg shell_rg23.89
Envelope Rg envelope_rg17.60
Shape Rg shape_rg17.38
Total Rg total_rg18.39
Total atoms total_atoms1953
Residues n_residues253
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 dmax57.7
Rg (real space) rg_real18.48
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real1.3430e+07
I(0) uncertainty (real space) i0_real_error1.6360e+05
Rg (reciprocal space) rg_reciprocal18.50
I(0) (reciprocal space) i0_reciprocal13430000.0000
Solution quality estimate total_estimate0.8944
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.7
Skewness Skewness skewness0.089
Kurtosis Kurtosis kurtosis-0.476
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3200000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.955

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)