9ces

Guillardia theta Fanzor (GtFz) State 2

Method: ELECTRON MICROSCOPY Dmax: 128.8 Å Quality: GOOD

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

Maltose/maltodextrin-binding periplasmic protein,Guillardia theta Fanzor1

Guillardia theta

UniProt L1JXG4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 DNA 2 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain P; UniProt 2–690 Not recorded ;DNA (5'-D(P*CP*CP*CP*GP*GP*GP*GP*CP*CP*TP*TP*TP*AP*AP*G)-3') ; × 1 ;DNA (5'-D(P*AP*TP*GP*AP*CP*TP*TP*CP*TP*CP*TP*TP*AP*AP*AP*GP*GP*CP*CP*CP*CP*GP*GP*G)-3') ; × 1 RNA (142-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.28 Å

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name L1JXG4_GUITC
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 412–1100; UniProt 2–690

Maltose/maltodextrin-binding periplasmic protein,Guillardia theta Fanzor1

Guillardia theta

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 DNA 2 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain P; UniProt 27–392 Not recorded ;DNA (5'-D(P*CP*CP*CP*GP*GP*GP*GP*CP*CP*TP*TP*TP*AP*AP*G)-3') ; × 1 ;DNA (5'-D(P*AP*TP*GP*AP*CP*TP*TP*CP*TP*CP*TP*TP*AP*AP*AP*GP*GP*CP*CP*CP*CP*GP*GP*G)-3') ; × 1 RNA (142-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.28 Å

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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 19–384; UniProt 27–392

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 9ces

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ces
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ces
Deposition date deposition_date2024-06-27
Structure title titleGuillardia theta Fanzor (GtFz) State 2
Keywords keywordsFanzor, Eukaryotic, RNA-guided, nuclease, Gene editing, RNA BINDING PROTEIN-RNA-DNA complex; RNA BINDING PROTEIN/RNA/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.05
Radius of gyration Rg (electron density) rg_electron34.86
Forward intensity I(0) i0334459000.00
Molecular weight molecular_weight114760.0 kDa
Excluded volume excluded_volume129750 ų
Envelope volume envelope_volume195800 ų
Hydration-shell volume shell_volume47872 ų
Envelope diameter envelope_diameter138.4
Shell Rg shell_rg40.57
Envelope Rg envelope_rg35.23
Shape Rg shape_rg34.77
Total Rg total_rg35.39
Total atoms total_atoms14363
Residues n_residues745
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 dmax128.8
Rg (real space) rg_real36.16
Rg uncertainty (real space) rg_real_error1.43
I(0) (real space) i0_real3.3450e+08
I(0) uncertainty (real space) i0_real_error6.4380e+06
Rg (reciprocal space) rg_reciprocal36.09
I(0) (reciprocal space) i0_reciprocal334400000.0000
Solution quality estimate total_estimate0.8506
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.0
Skewness Skewness skewness0.494
Kurtosis Kurtosis kurtosis0.056
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26240000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.733; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.952; Smooth: 0.902

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)