11qc

Human transferrin receptor ectodomain

Method: ELECTRON MICROSCOPY Dmax: 113.8 Å Quality: REASONABLE

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

Transferrin receptor protein 1, serum form

Homo sapiens

UniProt P02786

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 122–760 Chain B; UniProt 122–760 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.40 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.

23 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TFR1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–639; UniProt 122–760 Author chain B; PDBConstruct 1–639; UniProt 122–760

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 11qc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 11qc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id11qc
Deposition date deposition_date2026-03-10
Structure title titleHuman transferrin receptor ectodomain
Keywords keywordsTfR, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.26
Radius of gyration Rg (electron density) rg_electron34.44
Forward intensity I(0) i0304456000.00
Molecular weight molecular_weight144300.0 kDa
Excluded volume excluded_volume181910 ų
Envelope volume envelope_volume229070 ų
Hydration-shell volume shell_volume54441 ų
Envelope diameter envelope_diameter112.1
Shell Rg shell_rg41.79
Envelope Rg envelope_rg34.24
Shape Rg shape_rg34.37
Total Rg total_rg35.20
Total atoms total_atoms10198
Residues n_residues1278
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 dmax113.8
Rg (real space) rg_real35.19
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real3.0450e+08
I(0) uncertainty (real space) i0_real_error4.0580e+06
Rg (reciprocal space) rg_reciprocal35.24
I(0) (reciprocal space) i0_reciprocal304500000.0000
Solution quality estimate total_estimate0.6763
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.0
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.424
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha102900000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.999; Smooth: 0.932

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)