9thq

Crystal structure of the human serum transferrin with Fe(III) bound at the C-lobe only

Method: X-RAY DIFFRACTION Dmax: 92.0 Å Quality: EXCELLENT

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain AAA; UniProt 20–698 Not recorded FE FE (III) ION × 1 MLA MALONIC ACID × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 GOL GLYCEROL × 1 BCT BICARBONATE ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;15% (w/v) PEG 3350, 16% (v/v) glycerol, 8 mM disodium malonate, 150 mM Na-PIPES pH 6.5 Resolution 2.44 Å R-free 0.231

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 AAA; PDBConstruct 1–679; 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 9thq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9thq
Deposition date deposition_date2025-12-03
Structure title titleCrystal structure of the human serum transferrin with Fe(III) bound at the C-lobe only
Keywords keywordsprotein metalation, vanadium compounds, METAL TRANSPORT; METAL TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.37
Radius of gyration Rg (electron density) rg_electron28.45
Forward intensity I(0) i098073200.00
Molecular weight molecular_weight75257.0 kDa
Excluded volume excluded_volume92969 ų
Envelope volume envelope_volume115210 ų
Hydration-shell volume shell_volume33967 ų
Envelope diameter envelope_diameter95.4
Shell Rg shell_rg35.53
Envelope Rg envelope_rg28.31
Shape Rg shape_rg28.45
Total Rg total_rg29.11
Total atoms total_atoms5265
Residues n_residues670
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 dmax92.0
Rg (real space) rg_real29.32
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real9.8070e+07
I(0) uncertainty (real space) i0_real_error1.4660e+06
Rg (reciprocal space) rg_reciprocal29.35
I(0) (reciprocal space) i0_reciprocal98080000.0000
Solution quality estimate total_estimate0.9071
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.4
Skewness Skewness skewness0.242
Kurtosis Kurtosis kurtosis-0.548
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21100000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)