9cdq

Transferrin Binding Protein A in complex with transferrin (iron bound in N lobe only)

Method: ELECTRON MICROSCOPY Dmax: 140.8 Å Quality: GOOD

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

Serotransferrin

OrganismNot specified

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 1–698 Not recorded Transferrin-binding protein A × 1 (Q9K0U9) BCT BICARBONATE ION × 1 FE FE (III) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.76 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.

64 other PDB entries and 94 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRFE_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain F; PDBConstruct 1–698; UniProt 1–698

Transferrin-binding protein A

Neisseria meningitidis serogroup B

UniProt Q9K0U9

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 25–915 Not recorded Serotransferrin × 1 (P02787) BCT BICARBONATE ION × 1 FE FE (III) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.76 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBPA_NEIMB
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 25–915; UniProt 25–915

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 9cdq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9cdq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9cdq
Deposition date deposition_date2024-06-25
Structure title titleTransferrin Binding Protein A in complex with transferrin (iron bound in N lobe only)
Keywords keywordsMembrane protein, metal transporter, iron import, ton B-dependent transporter, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.01
Radius of gyration Rg (electron density) rg_electron43.33
Forward intensity I(0) i0464511000.00
Molecular weight molecular_weight170880.0 kDa
Excluded volume excluded_volume211250 ų
Envelope volume envelope_volume290310 ų
Hydration-shell volume shell_volume58131 ų
Envelope diameter envelope_diameter147.5
Shell Rg shell_rg46.04
Envelope Rg envelope_rg42.89
Shape Rg shape_rg43.34
Total Rg total_rg43.39
Total atoms total_atoms12032
Residues n_residues1545
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 dmax140.8
Rg (real space) rg_real43.17
Rg uncertainty (real space) rg_real_error1.71
I(0) (real space) i0_real4.6450e+08
I(0) uncertainty (real space) i0_real_error8.6120e+06
Rg (reciprocal space) rg_reciprocal43.01
I(0) (reciprocal space) i0_reciprocal464400000.0000
Solution quality estimate total_estimate0.8637
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.9
Skewness Skewness skewness0.394
Kurtosis Kurtosis kurtosis-0.521
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha73260000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.868; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.660

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)