7oaf

conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A, crystal form III

Method: X-RAY DIFFRACTION Dmax: 126.5 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, mutant beta1/A,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 Chain B; UniProt 311–335 Chain C; UniProt 311–335 Not recorded 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1M tri-sodium citrate pH 4.5, 9.3% PEG 6000 Resolution 1.45 Å R-free 0.215

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 Author chain B; PDBConstruct 34–58; UniProt 311–335 Author chain C; 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, mutant beta1/A,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 Chain B; UniProt 250–277 Chain B; UniProt 250–277 Chain C; UniProt 250–277 Chain C; UniProt 250–277 Not recorded 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1M tri-sodium citrate pH 4.5, 9.3% PEG 6000 Resolution 1.45 Å R-free 0.215

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 Author chain B; PDBConstruct 6–33; UniProt 250–277 Author chain B; PDBConstruct 59–86; UniProt 250–277 Author chain C; PDBConstruct 6–33; UniProt 250–277 Author chain C; 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 7oaf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7oaf
Deposition date deposition_date2021-04-19
Structure title titleconserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A, crystal form III
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_guinier33.94
Radius of gyration Rg (electron density) rg_electron35.56
Forward intensity I(0) i012801800.00
Molecular weight molecular_weight29225.0 kDa
Excluded volume excluded_volume37368 ų
Envelope volume envelope_volume50554 ų
Hydration-shell volume shell_volume15347 ų
Envelope diameter envelope_diameter123.1
Shell Rg shell_rg31.82
Envelope Rg envelope_rg36.70
Shape Rg shape_rg35.43
Total Rg total_rg35.65
Total atoms total_atoms4238
Residues n_residues243
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 dmax126.5
Rg (real space) rg_real34.81
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real1.2800e+07
I(0) uncertainty (real space) i0_real_error2.5000e+05
Rg (reciprocal space) rg_reciprocal34.27
I(0) (reciprocal space) i0_reciprocal12800000.0000
Solution quality estimate total_estimate0.5508
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary18.8
Skewness Skewness skewness0.706
Kurtosis Kurtosis kurtosis-0.342
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha765100.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.051; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.005; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)