3fgs

Crystal structure of G65R/K206E double mutant of the N-lobe human transferrin

Method: X-RAY DIFFRACTION Dmax: 68.5 Å Quality: GOOD

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 20–356 Fragment:Peptidase S60 1 domain Mutation:G65R, K206E CO3 CARBONATE ION × 1 FE FE (III) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.7;293 K;200 mM potassium acetate buffer (pH 7.7) containing 10 mM KCl and 18% polyethylene glycol 3350. Concentration of the mutant was 17.5 mg/mL. Crystals appeared in approximately a week following micro-seeding with wild-type N-lobe, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.80 Å R-free 0.246

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 1–337; UniProt 20–356

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 3fgs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3fgs
Deposition date deposition_date2008-12-08
Structure title titleCrystal structure of G65R/K206E double mutant of the N-lobe human transferrin
Keywords keywords;Human transferrin, Iron binding protein, Dilysine pair, Disease mutation, Glycoprotein, Ion transport, Iron, Iron transport, Metal-binding, Methylation, Phosphoprotein, Polymorphism, Secreted, Transport, 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_guinier20.61
Radius of gyration Rg (electron density) rg_electron19.50
Forward intensity I(0) i023843300.00
Molecular weight molecular_weight36557.0 kDa
Excluded volume excluded_volume45390 ų
Envelope volume envelope_volume51894 ų
Hydration-shell volume shell_volume21887 ų
Envelope diameter envelope_diameter67.7
Shell Rg shell_rg26.28
Envelope Rg envelope_rg19.75
Shape Rg shape_rg19.47
Total Rg total_rg20.45
Total atoms total_atoms2562
Residues n_residues329
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 dmax68.5
Rg (real space) rg_real20.52
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real2.3840e+07
I(0) uncertainty (real space) i0_real_error2.5380e+05
Rg (reciprocal space) rg_reciprocal20.54
I(0) (reciprocal space) i0_reciprocal23840000.0000
Solution quality estimate total_estimate0.8790
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.8
Skewness Skewness skewness0.252
Kurtosis Kurtosis kurtosis-0.322
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha4989000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.808; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3fgsa_
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.94.1.2 — Transferrin

CATH v4.4 (2 domains)

Domain ID domain_id3fgsA01
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_id3fgsA02
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)