7oaa

conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors

Method: X-RAY DIFFRACTION Dmax: 124.8 Å Quality: REASONABLE

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

;General control transcription factor GCN4,conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors,General control transcription factor GCN4 ;

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt A0A0N0D484

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 Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 311–335 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1M HEPES pH 7.5, 30% (w/v) PEG 300 Resolution 1.40 Å R-free 0.269

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0N0D484_9DELT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 34–58; UniProt 311–335

;General control transcription factor GCN4,conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors,General control transcription factor GCN4 ;

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P03069

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 Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 250–277 Chain A; UniProt 250–277 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1M HEPES pH 7.5, 30% (w/v) PEG 300 Resolution 1.40 Å R-free 0.269

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.

162 other PDB entries and 200 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCN4_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–33; UniProt 250–277 Author chain A; PDBConstruct 59–86; UniProt 250–277

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 7oaa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7oaa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7oaa
Deposition date deposition_date2021-04-19
Structure title titleconserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors
Keywords keywordsCoiled Coil, beta layer, hexad repeat, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.16
Radius of gyration Rg (electron density) rg_electron35.63
Forward intensity I(0) i01544920.00
Molecular weight molecular_weight9863.0 kDa
Excluded volume excluded_volume12661 ų
Envelope volume envelope_volume20881 ų
Hydration-shell volume shell_volume6697 ų
Envelope diameter envelope_diameter124.3
Shell Rg shell_rg29.79
Envelope Rg envelope_rg35.70
Shape Rg shape_rg35.49
Total Rg total_rg35.34
Total atoms total_atoms1435
Residues n_residues82
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 dmax124.8
Rg (real space) rg_real34.48
Rg uncertainty (real space) rg_real_error2.10
I(0) (real space) i0_real1.5450e+06
I(0) uncertainty (real space) i0_real_error2.9800e+04
Rg (reciprocal space) rg_reciprocal33.92
I(0) (reciprocal space) i0_reciprocal1544000.0000
Solution quality estimate total_estimate0.5404
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary7.8
Skewness Skewness skewness0.598
Kurtosis Kurtosis kurtosis-0.453
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha87870.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.001; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.019; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)