8k1d

SID1 transmembrane family member 1

Method: ELECTRON MICROSCOPY Dmax: 91.3 Å Quality: EXCELLENT

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

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 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 301–827 Chain B; UniProt 301–827 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.53 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 1–484; UniProt 301–827 Author chain B; PDBConstruct 1–484; UniProt 301–827

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 8k1d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8k1d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8k1d
Deposition date deposition_date2023-07-10
Structure title titleSID1 transmembrane family member 1
Keywords keywordsVIRAL PROTEIN-IMMUNE SYSTEM COMPLEX, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.43
Radius of gyration Rg (electron density) rg_electron28.88
Forward intensity I(0) i062749900.00
Molecular weight molecular_weight69299.0 kDa
Excluded volume excluded_volume89862 ų
Envelope volume envelope_volume122150 ų
Hydration-shell volume shell_volume35377 ų
Envelope diameter envelope_diameter93.5
Shell Rg shell_rg35.93
Envelope Rg envelope_rg28.69
Shape Rg shape_rg28.84
Total Rg total_rg29.91
Total atoms total_atoms4902
Residues n_residues610
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 dmax91.3
Rg (real space) rg_real29.35
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real6.2750e+07
I(0) uncertainty (real space) i0_real_error9.4820e+05
Rg (reciprocal space) rg_reciprocal29.38
I(0) (reciprocal space) i0_reciprocal62750000.0000
Solution quality estimate total_estimate0.9118
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.190
Kurtosis Kurtosis kurtosis-0.552
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8422000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.966; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.954

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)