3s9n

Complex between transferrin receptor 1 and transferrin with iron in the N-Lobe, room temperature

Method: X-RAY DIFFRACTION Dmax: 164.8 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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 120–760 Fragment:UNP residues 120-760 Serotransferrin × 2 (P02787) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 2 FE FE (III) ION × 2 CO3 CARBONATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;5% PEG 3350, 0.2 M MgCl2, 10% 1,2-propanediol, pH Hepes 7.5, vapor diffusion, hanging drop, temperature 293K Resolution 3.25 Å R-free 0.289
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 120–760 Fragment:UNP residues 120-760 Serotransferrin × 2 (P02787) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 2 FE FE (III) ION × 2 CO3 CARBONATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;5% PEG 3350, 0.2 M MgCl2, 10% 1,2-propanediol, pH Hepes 7.5, vapor diffusion, hanging drop, temperature 293K Resolution 3.25 Å R-free 0.289

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 32 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 14–654; UniProt 120–760 Author chain B; PDBConstruct 14–654; UniProt 120–760

Serotransferrin

Homo sapiens

UniProt P02787

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 20–698 Fragment:UNP residues 20-698 Mutation:N427D, Y531F Transferrin receptor protein 1 × 2 (P02786) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 2 FE FE (III) ION × 2 CO3 CARBONATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;5% PEG 3350, 0.2 M MgCl2, 10% 1,2-propanediol, pH Hepes 7.5, vapor diffusion, hanging drop, temperature 293K Resolution 3.25 Å R-free 0.289
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 20–698 Fragment:UNP residues 20-698 Mutation:N427D, Y531F Transferrin receptor protein 1 × 2 (P02786) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 2 FE FE (III) ION × 2 CO3 CARBONATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;5% PEG 3350, 0.2 M MgCl2, 10% 1,2-propanediol, pH Hepes 7.5, vapor diffusion, hanging drop, temperature 293K Resolution 3.25 Å R-free 0.289

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.

64 other PDB entries and 93 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRFE_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 15–693; UniProt 20–698 Author chain D; PDBConstruct 15–693; UniProt 20–698

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 3s9n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3s9n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3s9n
Deposition date deposition_date2011-06-01
Structure title titleComplex between transferrin receptor 1 and transferrin with iron in the N-Lobe, room temperature
Keywords keywordsTransferrin receptor complex, transferrin superfamily, carboxypeptidase like, Transport Protein; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier49.19
Radius of gyration Rg (electron density) rg_electron48.74
Forward intensity I(0) i0819877000.00
Molecular weight molecular_weight231350.0 kDa
Excluded volume excluded_volume286210 ų
Envelope volume envelope_volume426570 ų
Hydration-shell volume shell_volume74031 ų
Envelope diameter envelope_diameter168.3
Shell Rg shell_rg51.79
Envelope Rg envelope_rg47.88
Shape Rg shape_rg48.74
Total Rg total_rg48.83
Total atoms total_atoms16304
Residues n_residues2245
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 dmax164.8
Rg (real space) rg_real49.35
Rg uncertainty (real space) rg_real_error1.48
I(0) (real space) i0_real8.1990e+08
I(0) uncertainty (real space) i0_real_error1.6250e+07
Rg (reciprocal space) rg_reciprocal49.19
I(0) (reciprocal space) i0_reciprocal819700000.0000
Solution quality estimate total_estimate0.8767
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.5
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.546
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha78250000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.758

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id3s9nA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3s9nA02
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id3s9nA03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology930 — Transcription Elongation Factor S-II; Chain A
Homologous superfamily homologous superfamily40 — Transferrin receptor-like, dimerisation domain
Domain ID domain_id3s9nB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3s9nB02
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id3s9nB03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology930 — Transcription Elongation Factor S-II; Chain A
Homologous superfamily homologous superfamily40 — Transferrin receptor-like, dimerisation domain
Domain ID domain_id3s9nC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id3s9nC02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id3s9nC03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id3s9nD01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id3s9nD02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id3s9nD03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II

8. Citations (1)

9. Files and Curves (10)