2o7u

Crystal structure of K206E/K296E mutant of the N-terminal half molecule of human transferrin

Method: X-RAY DIFFRACTION Dmax: 148.3 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 B; UniProt 20–356 Fragment:N-lobe Mutation:K206E, K296E FE FE (III) ION × 1 CO3 CARBONATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;291 K;Protein: 35mg/ml, 0.1M ammonium bicarbonate. Well: 20% PEG 3350, 0.2 M potassium acetate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.80 Å R-free 0.259
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 20–356 Fragment:N-lobe Mutation:K206E, K296E FE FE (III) ION × 1 CO3 CARBONATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;291 K;Protein: 35mg/ml, 0.1M ammonium bicarbonate. Well: 20% PEG 3350, 0.2 M potassium acetate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.80 Å R-free 0.259
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 20–356 Fragment:N-lobe Mutation:K206E, K296E FE FE (III) ION × 1 CO3 CARBONATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;291 K;Protein: 35mg/ml, 0.1M ammonium bicarbonate. Well: 20% PEG 3350, 0.2 M potassium acetate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.80 Å R-free 0.259
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 20–356 Fragment:N-lobe Mutation:K206E, K296E FE FE (III) ION × 1 CO3 CARBONATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;291 K;Protein: 35mg/ml, 0.1M ammonium bicarbonate. Well: 20% PEG 3350, 0.2 M potassium acetate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.80 Å R-free 0.259
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 20–356 Fragment:N-lobe Mutation:K206E, K296E FE FE (III) ION × 1 CO3 CARBONATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;291 K;Protein: 35mg/ml, 0.1M ammonium bicarbonate. Well: 20% PEG 3350, 0.2 M potassium acetate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.80 Å R-free 0.259
6 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain F; UniProt 20–356 Fragment:N-lobe Mutation:K206E, K296E FE FE (III) ION × 1 CO3 CARBONATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;291 K;Protein: 35mg/ml, 0.1M ammonium bicarbonate. Well: 20% PEG 3350, 0.2 M potassium acetate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.80 Å R-free 0.259
7 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain G; UniProt 20–356 Fragment:N-lobe Mutation:K206E, K296E FE FE (III) ION × 1 CO3 CARBONATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;291 K;Protein: 35mg/ml, 0.1M ammonium bicarbonate. Well: 20% PEG 3350, 0.2 M potassium acetate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.80 Å R-free 0.259
8 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain H; UniProt 20–356 Fragment:N-lobe Mutation:K206E, K296E FE FE (III) ION × 1 CO3 CARBONATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;291 K;Protein: 35mg/ml, 0.1M ammonium bicarbonate. Well: 20% PEG 3350, 0.2 M potassium acetate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.80 Å R-free 0.259
9 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain I; UniProt 20–356 Fragment:N-lobe Mutation:K206E, K296E FE FE (III) ION × 1 CO3 CARBONATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;291 K;Protein: 35mg/ml, 0.1M ammonium bicarbonate. Well: 20% PEG 3350, 0.2 M potassium acetate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.80 Å R-free 0.259

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 86 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 Author chain B; PDBConstruct 1–337; UniProt 20–356 Author chain C; PDBConstruct 1–337; UniProt 20–356 Author chain D; PDBConstruct 1–337; UniProt 20–356 Author chain E; PDBConstruct 1–337; UniProt 20–356 Author chain F; PDBConstruct 1–337; UniProt 20–356 Author chain G; PDBConstruct 1–337; UniProt 20–356 Author chain H; PDBConstruct 1–337; UniProt 20–356 Author chain I; 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 2o7u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2o7u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2o7u
Deposition date deposition_date2006-12-11
Structure title titleCrystal structure of K206E/K296E mutant of the N-terminal half molecule of human transferrin
Keywords keywordsHuman transferrin, Iron binding protein, Dilysine pair, 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_guinier47.60
Radius of gyration Rg (electron density) rg_electron46.95
Forward intensity I(0) i01624670000.00
Molecular weight molecular_weight328110.0 kDa
Excluded volume excluded_volume407060 ų
Envelope volume envelope_volume561640 ų
Hydration-shell volume shell_volume96546 ų
Envelope diameter envelope_diameter153.7
Shell Rg shell_rg53.93
Envelope Rg envelope_rg45.73
Shape Rg shape_rg46.94
Total Rg total_rg47.23
Total atoms total_atoms22995
Residues n_residues2961
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 dmax148.3
Rg (real space) rg_real47.25
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real1.6250e+09
I(0) uncertainty (real space) i0_real_error2.8540e+07
Rg (reciprocal space) rg_reciprocal47.60
I(0) (reciprocal space) i0_reciprocal1625000000.0000
Solution quality estimate total_estimate0.8938
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.9
Skewness Skewness skewness0.065
Kurtosis Kurtosis kurtosis-0.540
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha89160000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.896

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 27 domains

SCOP 2.08 (9 domains)

Domain ID domain_idd2o7ua_
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
Domain ID domain_idd2o7ub_
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
Domain ID domain_idd2o7uc_
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
Domain ID domain_idd2o7ud_
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
Domain ID domain_idd2o7ue_
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
Domain ID domain_idd2o7uf_
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
Domain ID domain_idd2o7ug_
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
Domain ID domain_idd2o7uh_
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
Domain ID domain_idd2o7ui_
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 (18 domains)

Domain ID domain_id2o7uA01
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_id2o7uA02
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_id2o7uB01
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_id2o7uB02
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_id2o7uC01
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_id2o7uC02
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_id2o7uD01
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_id2o7uD02
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_id2o7uE01
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_id2o7uE02
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_id2o7uF01
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_id2o7uF02
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_id2o7uG01
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_id2o7uG02
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_id2o7uH01
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_id2o7uH02
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_id2o7uI01
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_id2o7uI02
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)