6lf3

3D domain-swapped dimer of the maltose-binding protein fused to a fragment of the protein-tyrosine kinase 2-beta

Method: X-RAY DIFFRACTION Dmax: 138.9 Å Quality: REASONABLE

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

Maltose/maltodextrin-binding periplasmic protein,Protein-tyrosine kinase 2-beta

Homo sapiens

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–392 Chain B; UniProt 27–392 Mutation:surface entropy reduction mutant, D83A,K84A,E173A,N174A,K240A,E360A,K363A,D364A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 10.5;298 K;30% (v/v) PEG 400, 0.1M CAPS/Sodium hydroxide Resolution 3.20 Å R-free 0.284
2 Insufficient information Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 27–392 Chain D; UniProt 27–392 Mutation:surface entropy reduction mutant, D83A,K84A,E173A,N174A,K240A,E360A,K363A,D364A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 10.5;298 K;30% (v/v) PEG 400, 0.1M CAPS/Sodium hydroxide Resolution 3.20 Å R-free 0.284
3 Insufficient information Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 27–392 Chain F; UniProt 27–392 Mutation:surface entropy reduction mutant, D83A,K84A,E173A,N174A,K240A,E360A,K363A,D364A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 10.5;298 K;30% (v/v) PEG 400, 0.1M CAPS/Sodium hydroxide Resolution 3.20 Å R-free 0.284

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.

366 other PDB entries and 489 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–367; UniProt 27–392 Author chain B; PDBConstruct 2–367; UniProt 27–392 Author chain C; PDBConstruct 2–367; UniProt 27–392 Author chain D; PDBConstruct 2–367; UniProt 27–392 Author chain E; PDBConstruct 2–367; UniProt 27–392 Author chain F; PDBConstruct 2–367; UniProt 27–392

Maltose/maltodextrin-binding periplasmic protein,Protein-tyrosine kinase 2-beta

Homo sapiens

UniProt Q14289

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 790–839 Chain B; UniProt 790–839 Mutation:surface entropy reduction mutant, D83A,K84A,E173A,N174A,K240A,E360A,K363A,D364A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 10.5;298 K;30% (v/v) PEG 400, 0.1M CAPS/Sodium hydroxide Resolution 3.20 Å R-free 0.284
2 Insufficient information Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 790–839 Chain D; UniProt 790–839 Mutation:surface entropy reduction mutant, D83A,K84A,E173A,N174A,K240A,E360A,K363A,D364A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 10.5;298 K;30% (v/v) PEG 400, 0.1M CAPS/Sodium hydroxide Resolution 3.20 Å R-free 0.284
3 Insufficient information Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 790–839 Chain F; UniProt 790–839 Mutation:surface entropy reduction mutant, D83A,K84A,E173A,N174A,K240A,E360A,K363A,D364A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 10.5;298 K;30% (v/v) PEG 400, 0.1M CAPS/Sodium hydroxide Resolution 3.20 Å R-free 0.284

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.

24 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FAK2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 370–419; UniProt 790–839 Author chain B; PDBConstruct 370–419; UniProt 790–839 Author chain C; PDBConstruct 370–419; UniProt 790–839 Author chain D; PDBConstruct 370–419; UniProt 790–839 Author chain E; PDBConstruct 370–419; UniProt 790–839 Author chain F; PDBConstruct 370–419; UniProt 790–839

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 6lf3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6lf3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6lf3
Deposition date deposition_date2019-11-28
Structure title title3D domain-swapped dimer of the maltose-binding protein fused to a fragment of the protein-tyrosine kinase 2-beta
Keywords keywords;maltose binding protein, domain-swapping, arm exchange, folding, passenger protein, surface entropy reduction, fixed-arm carrier, dimer, PYK2, apo-protein, SUGAR BINDING PROTEIN ;; SUGAR BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier46.16
Radius of gyration Rg (electron density) rg_electron45.46
Forward intensity I(0) i0795666000.00
Molecular weight molecular_weight242180.0 kDa
Excluded volume excluded_volume306370 ų
Envelope volume envelope_volume405870 ų
Hydration-shell volume shell_volume74248 ų
Envelope diameter envelope_diameter147.9
Shell Rg shell_rg50.60
Envelope Rg envelope_rg44.07
Shape Rg shape_rg45.43
Total Rg total_rg45.79
Total atoms total_atoms17124
Residues n_residues2210
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 dmax138.9
Rg (real space) rg_real45.90
Rg uncertainty (real space) rg_real_error1.14
I(0) (real space) i0_real7.9570e+08
I(0) uncertainty (real space) i0_real_error1.6730e+07
Rg (reciprocal space) rg_reciprocal46.16
I(0) (reciprocal space) i0_reciprocal795900000.0000
Solution quality estimate total_estimate0.6709
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.3
Skewness Skewness skewness0.074
Kurtosis Kurtosis kurtosis-0.595
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44010000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.974; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.989; Smooth: 0.461

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)