SAXSdb — 6lf3

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

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

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 2 其他Polymer 2	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2	Consistent with protein count
2	Insufficient information	Homooligomer	Protein 2 其他Polymer 2	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2	Consistent with protein count
3	Insufficient information	Homooligomer	Protein 2 其他Polymer 2	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 2 其他Polymer 2	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2	Consistent with protein count
2	Insufficient information	Homooligomer	Protein 2 其他Polymer 2	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2	Consistent with protein count
3	Insufficient information	Homooligomer	Protein 2 其他Polymer 2	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2	Consistent with protein count

Other States of the Same Protein in the Database

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6lf3
Deposition date deposition_date	2019-11-28
Structure title title	3D 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 method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

6lf3__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

6lf3__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6lf3__assembly_2__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	30.43 Å
Rg (electron density)	29.48 Å
Total Rg	30.31 Å
Atom count	5702
Residues	736
Excluded volume	102030 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6lf3__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`6lf3__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`6lf3__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Maltose/maltodextrin-binding periplasmic protein,Protein-tyrosine kinase 2-beta
Molecular weight formula_weight	46397.6 kDa
EC 编号 ec_number	2.7.10.2
Mutation mutation	surface entropy reduction mutant, D83A,K84A,E173A,N174A,K240A,E360A,K363A,D364A
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	17124

MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSAVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALAAAQTNAREEAQQLWEAEKVKMRQILDKQQKQMVEDYQWLRQEEKSLDPMVYMNDKS

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 branched

Description description	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose
Molecular weight formula_weight	342.3 kDa
Source method src_method	man
Copy count entity_count	6

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Unit-cell length a length_a	78.780 Å
Unit-cell length b length_b	92.740 Å
Unit-cell length c length_c	93.610 Å
Unit-cell angle α angle_alpha	112.46 °
Unit-cell angle β angle_beta	101.66 °
Unit-cell angle γ angle_gamma	94.93 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	3.200 Å
Low-resolution limit resolution_low	47.900 Å
R factor r_factor	0.2459
R_work r_work	0.2439
R_free r_free	0.2839

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

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

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

State in the Current Structure

Other States of the Same Protein in the Database

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

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

6lf3__assembly_2__model_1

6lf3__assembly_2__model_1 | I(q)

6lf3__assembly_2__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 branched

7. Citations (1)

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

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

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

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

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

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

6lf3__assembly_2__model_1

6lf3__assembly_2__model_1 | I(q)

6lf3__assembly_2__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 branched

7. Citations (1)