8j6m

SIDT1 protein

Method: ELECTRON MICROSCOPY Dmax: 127.0 Å Quality: GOOD

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

Green fluorescent protein,SID1 transmembrane family member 1

Homo sapiens

UniProt A0A059PIQ0

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 3–236 Chain B; UniProt 3–236 Not recorded CLR CHOLESTEROL × 8 ZN ZINC ION × 2 NA SODIUM ION × 1 OLA OLEIC ACID × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.77 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.

91 other PDB entries and 137 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A059PIQ0_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 50–283; UniProt 3–236 Author chain B; PDBConstruct 50–283; UniProt 3–236

Green fluorescent protein,SID1 transmembrane family member 1

Homo sapiens

UniProt Q9NXL6

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 20–827 Chain B; UniProt 20–827 Not recorded CLR CHOLESTEROL × 8 ZN ZINC ION × 2 NA SODIUM ION × 1 OLA OLEIC ACID × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.77 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIDT1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 291–1098; UniProt 20–827 Author chain B; PDBConstruct 291–1098; UniProt 20–827

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 8j6m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8j6m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8j6m
Deposition date deposition_date2023-04-26
Structure title titleSIDT1 protein
Keywords keywordstransport T1, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.35
Radius of gyration Rg (electron density) rg_electron36.90
Forward intensity I(0) i0271005000.00
Molecular weight molecular_weight149630.0 kDa
Excluded volume excluded_volume193580 ų
Envelope volume envelope_volume237120 ų
Hydration-shell volume shell_volume53121 ų
Envelope diameter envelope_diameter124.3
Shell Rg shell_rg43.00
Envelope Rg envelope_rg37.08
Shape Rg shape_rg36.89
Total Rg total_rg37.36
Total atoms total_atoms10579
Residues n_residues1282
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 dmax127.0
Rg (real space) rg_real37.41
Rg uncertainty (real space) rg_real_error1.40
I(0) (real space) i0_real2.7100e+08
I(0) uncertainty (real space) i0_real_error4.9960e+06
Rg (reciprocal space) rg_reciprocal37.37
I(0) (reciprocal space) i0_reciprocal271000000.0000
Solution quality estimate total_estimate0.8824
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.3
Skewness Skewness skewness0.380
Kurtosis Kurtosis kurtosis-0.375
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha55070000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.847; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.934

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)