2nsu

Crystal structure of the ectodomain of human transferrin receptor fitted into a cryo-EM reconstruction of canine parvovirus and feline transferrin receptor complex

Method: ELECTRON MICROSCOPY Dmax: 113.6 Å Quality: GOOD

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

Transferrin receptor protein 1

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 Fragment:THE ECTODOMAIN OF HUMAN TRANSFERRIN RECEPTOR No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:0.02M TRIS-HCL;pH 7.5;0.02M TRIS-HCL cryo-EM vitrification conditions:Cryogen ETHANE;PLUNGED IN LIQUID ETHANE Resolution 27.00 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 2nsu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2nsu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2nsu
Deposition date deposition_date2006-11-06
Structure title titleCrystal structure of the ectodomain of human transferrin receptor fitted into a cryo-EM reconstruction of canine parvovirus and feline transferrin receptor complex
Keywords keywordstransferrin receptor, virus-receptor complex, METAL TRANSPORT; METAL TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.94
Radius of gyration Rg (electron density) rg_electron34.14
Forward intensity I(0) i0297143000.00
Molecular weight molecular_weight143040.0 kDa
Excluded volume excluded_volume180350 ų
Envelope volume envelope_volume220600 ų
Hydration-shell volume shell_volume52787 ų
Envelope diameter envelope_diameter110.8
Shell Rg shell_rg41.75
Envelope Rg envelope_rg34.16
Shape Rg shape_rg34.06
Total Rg total_rg34.91
Total atoms total_atoms10112
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 dmax113.6
Rg (real space) rg_real34.89
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real2.9710e+08
I(0) uncertainty (real space) i0_real_error5.5460e+06
Rg (reciprocal space) rg_reciprocal34.92
I(0) (reciprocal space) i0_reciprocal297200000.0000
Solution quality estimate total_estimate0.8928
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.4
Skewness Skewness skewness0.316
Kurtosis Kurtosis kurtosis-0.427
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha88770000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.951

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd2nsua1
Class classa — All alpha proteins
Fold Fold folda.48 — N-cbl like
Superfamily Superfamily superfamilya.48.2 — Transferrin receptor-like dimerisation domain
Family Family familya.48.2.1 — Transferrin receptor-like dimerisation domain
Domain ID domain_idd2nsua2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.8 — The 'swivelling' beta/beta/alpha domain
Superfamily Superfamily superfamilyc.8.4 — PA domain
Family Family familyc.8.4.1 — PA domain
Domain ID domain_idd2nsua3
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.56 — Phosphorylase/hydrolase-like
Superfamily Superfamily superfamilyc.56.5 — Zn-dependent exopeptidases
Family Family familyc.56.5.5 — FolH catalytic domain-like
Domain ID domain_idd2nsub1
Class classa — All alpha proteins
Fold Fold folda.48 — N-cbl like
Superfamily Superfamily superfamilya.48.2 — Transferrin receptor-like dimerisation domain
Family Family familya.48.2.1 — Transferrin receptor-like dimerisation domain
Domain ID domain_idd2nsub2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.8 — The 'swivelling' beta/beta/alpha domain
Superfamily Superfamily superfamilyc.8.4 — PA domain
Family Family familyc.8.4.1 — PA domain
Domain ID domain_idd2nsub3
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.56 — Phosphorylase/hydrolase-like
Superfamily Superfamily superfamilyc.56.5 — Zn-dependent exopeptidases
Family Family familyc.56.5.5 — FolH catalytic domain-like

8. Citations (1)

9. Files and Curves (10)