8kcx

Cryo-EM structure of human SIDT1

Method: ELECTRON MICROSCOPY Dmax: 122.0 Å Quality: REASONABLE

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 Other combination Homooligomer Protein × 2 其他Polymer 8 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–827 Chain C; UniProt 1–827 Not recorded beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.96 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 1–827; UniProt 1–827 Author chain C; PDBConstruct 1–827; UniProt 1–827

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 8kcx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8kcx
Deposition date deposition_date2023-08-08
Structure title titleCryo-EM structure of human SIDT1
Keywords keywordsMembrane protein; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.53
Radius of gyration Rg (electron density) rg_electron36.31
Forward intensity I(0) i0235071000.00
Molecular weight molecular_weight134430.0 kDa
Excluded volume excluded_volume172350 ų
Envelope volume envelope_volume233830 ų
Hydration-shell volume shell_volume53033 ų
Envelope diameter envelope_diameter125.3
Shell Rg shell_rg42.89
Envelope Rg envelope_rg36.50
Shape Rg shape_rg36.29
Total Rg total_rg36.88
Total atoms total_atoms9486
Residues n_residues1142
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 dmax122.0
Rg (real space) rg_real36.58
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real2.3510e+08
I(0) uncertainty (real space) i0_real_error3.5350e+06
Rg (reciprocal space) rg_reciprocal36.55
I(0) (reciprocal space) i0_reciprocal235100000.0000
Solution quality estimate total_estimate0.6817
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.7
Skewness Skewness skewness0.401
Kurtosis Kurtosis kurtosis-0.329
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha55620000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 1.000; Sysdev: 0.159; Positv: 1.000; Valcen: 0.974; Smooth: 0.843

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)