1jqf

Human Transferrin N-Lobe Mutant H249Q

Method: X-RAY DIFFRACTION Dmax: 66.8 Å Quality: GOOD

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

TRANSFERRIN

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 20–353 Fragment:N-TERMINUS (Residues 20-353) Mutation:H249Q CO3 CARBONATE ION × 1 FE FE (III) ION × 1 K POTASSIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;291 K;Hanging drop. Protein solution 35 mg/ml protein in 0.1M ammonium bicarbonate pH 7.4. Reservoir solution 0.1M potassium acetate, pH 7.4, 20-25% PEG 3350. Equal volumes of protein and reservoir solutions mixed., VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.85 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 1–334; UniProt 20–353

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 1jqf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1jqf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1jqf
Deposition date deposition_date2001-08-06
Structure title titleHuman Transferrin N-Lobe Mutant H249Q
Keywords keywordsiron binding protein, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.54
Radius of gyration Rg (electron density) rg_electron19.48
Forward intensity I(0) i023330500.00
Molecular weight molecular_weight36444.0 kDa
Excluded volume excluded_volume45348 ų
Envelope volume envelope_volume51261 ų
Hydration-shell volume shell_volume21667 ų
Envelope diameter envelope_diameter67.0
Shell Rg shell_rg26.11
Envelope Rg envelope_rg19.73
Shape Rg shape_rg19.46
Total Rg total_rg20.40
Total atoms total_atoms2552
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 dmax66.8
Rg (real space) rg_real20.46
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real2.3330e+07
I(0) uncertainty (real space) i0_real_error2.9070e+05
Rg (reciprocal space) rg_reciprocal20.47
I(0) (reciprocal space) i0_reciprocal23330000.0000
Solution quality estimate total_estimate0.8875
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.2
Skewness Skewness skewness0.244
Kurtosis Kurtosis kurtosis-0.349
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4634000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.846; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1jqfa_
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_id1jqfA01
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_id1jqfA02
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)