6ctc

Crystal structure of human transferrin bound to Triferic FPC iron pyrophosphate

Method: X-RAY DIFFRACTION Dmax: 89.6 Å Quality: EXCELLENT

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 20–698 Not recorded FE FE (III) ION × 2 CO3 CARBONATE ION × 1 POP PYROPHOSPHATE 2- × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;Apo human transferrin (ProSpec pro-325 purified by Q-sepharose) at 56 mg/mL (0.76 mM) against Morpheus screen condition D4 12.5% PEG 1000, 12.5% PEG3350, 12.5% MPD, 0.02 M each 1,6-hexanediol, 1-butanol, RS-1,2-propanediol, 2-propanol, 1,4-butanediol, 1,3-propanediol, 0.1 M MES/imidazole pH 6.5, crystal tracking ID 246352d4, unique puck ID suv0-5 Resolution 2.60 Å R-free 0.253

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 A; 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 6ctc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ctc
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6ctc
Deposition date deposition_date2018-03-22
Structure title titleCrystal structure of human transferrin bound to Triferic FPC iron pyrophosphate
Keywords keywordsiron, pyrophosphate, transferrin, triferic iron, FPC, transfusion, blood, plasma, 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_guinier28.88
Radius of gyration Rg (electron density) rg_electron27.89
Forward intensity I(0) i091900400.00
Molecular weight molecular_weight72013.0 kDa
Excluded volume excluded_volume88527 ų
Envelope volume envelope_volume107950 ų
Hydration-shell volume shell_volume32498 ų
Envelope diameter envelope_diameter94.3
Shell Rg shell_rg34.94
Envelope Rg envelope_rg27.76
Shape Rg shape_rg27.91
Total Rg total_rg28.52
Total atoms total_atoms5041
Residues n_residues673
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 dmax89.6
Rg (real space) rg_real28.84
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real9.1900e+07
I(0) uncertainty (real space) i0_real_error1.4880e+06
Rg (reciprocal space) rg_reciprocal28.86
I(0) (reciprocal space) i0_reciprocal91900000.0000
Solution quality estimate total_estimate0.9032
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.9
Skewness Skewness skewness0.257
Kurtosis Kurtosis kurtosis-0.553
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21450000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.960; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.867

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6ctca1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.0 — automated matches
Domain ID domain_idd6ctca2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id6ctcA01
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_id6ctcA02
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_id6ctcA03
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_id6ctcA04
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)