9h49

Crystal structure of the adduct between human serum transferrin (apo-form) and cisplatin

Method: X-RAY DIFFRACTION Dmax: 161.2 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 20–698 Not recorded CIT CITRIC ACID × 3 PT PLATINUM (II) ION × 2 NH3 AMMONIA × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;20% w/v PEG 3350 and 200 mM ammonium citrate pH 7.0 Resolution 3.52 Å R-free 0.249
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 20–698 Not recorded CIT CITRIC ACID × 3 PT PLATINUM (II) ION × 2 NH3 AMMONIA × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;20% w/v PEG 3350 and 200 mM ammonium citrate pH 7.0 Resolution 3.52 Å R-free 0.249

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–679; UniProt 20–698 Author chain B; 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 9h49

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9h49
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9h49
Deposition date deposition_date2024-10-17
Structure title titleCrystal structure of the adduct between human serum transferrin (apo-form) and cisplatin
Keywords keywordsCisplatin, metallodrug, anticancer, metal complex, methionine/cisplatin adduct, 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_guinier44.76
Radius of gyration Rg (electron density) rg_electron44.87
Forward intensity I(0) i0374583000.00
Molecular weight molecular_weight151920.0 kDa
Excluded volume excluded_volume187160 ų
Envelope volume envelope_volume261450 ų
Hydration-shell volume shell_volume52028 ų
Envelope diameter envelope_diameter168.9
Shell Rg shell_rg45.15
Envelope Rg envelope_rg44.47
Shape Rg shape_rg44.83
Total Rg total_rg45.03
Total atoms total_atoms10586
Residues n_residues1353
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 dmax161.2
Rg (real space) rg_real45.28
Rg uncertainty (real space) rg_real_error2.29
I(0) (real space) i0_real3.7460e+08
I(0) uncertainty (real space) i0_real_error7.7170e+06
Rg (reciprocal space) rg_reciprocal44.76
I(0) (reciprocal space) i0_reciprocal374400000.0000
Solution quality estimate total_estimate0.7965
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.0
Skewness Skewness skewness0.615
Kurtosis Kurtosis kurtosis-0.059
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22550000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.700; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.680; Smooth: 0.572

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)