6bqt

Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and T360

Method: X-RAY DIFFRACTION

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

14-3-3 protein theta

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Insulin receptor substrate protein of 53 kDa, peptide (IRSp53) × 1 （Q9UQB8） 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 PENTAETHYLENE GLYCOL × 3 1,2-ETHANEDIOL × 1 TETRAETHYLENE GLYCOL × 1 GLYCEROL × 1 water × 3	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Insulin receptor substrate protein of 53 kDa, peptide (IRSp53) × 1 （Q9UQB8） 1,2-ETHANEDIOL × 1 TETRAETHYLENE GLYCOL × 2 TRIETHYLENE GLYCOL × 1 DI(HYDROXYETHYL)ETHER × 1 water × 3	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	Insulin receptor substrate protein of 53 kDa, peptide (IRSp53) × 1 （Q9UQB8） PENTAETHYLENE GLYCOL × 2 GLYCEROL × 1 water × 3	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 3	Insulin receptor substrate protein of 53 kDa, peptide (IRSp53) × 1 （Q9UQB8） PENTAETHYLENE GLYCOL × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	1433T_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–245； UniProt 1–245 Author chain B； PDBConstruct 1–245； UniProt 1–245 Author chain D； PDBConstruct 1–245； UniProt 1–245 Author chain E； PDBConstruct 1–245； UniProt 1–245 Author chain G； PDBConstruct 1–245； UniProt 1–245 Author chain H； PDBConstruct 1–245； UniProt 1–245 Author chain J； PDBConstruct 1–245； UniProt 1–245 Author chain K； PDBConstruct 1–245； UniProt 1–245

Insulin receptor substrate protein of 53 kDa, peptide (IRSp53)

OrganismNot specified

UniProt Q9UQB8

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	14-3-3 protein theta × 2 （P27348） 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 PENTAETHYLENE GLYCOL × 3 1,2-ETHANEDIOL × 1 TETRAETHYLENE GLYCOL × 1 GLYCEROL × 1 water × 3	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	14-3-3 protein theta × 2 （P27348） 1,2-ETHANEDIOL × 1 TETRAETHYLENE GLYCOL × 2 TRIETHYLENE GLYCOL × 1 DI(HYDROXYETHYL)ETHER × 1 water × 3	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	14-3-3 protein theta × 2 （P27348） PENTAETHYLENE GLYCOL × 2 GLYCEROL × 1 water × 3	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 3	14-3-3 protein theta × 2 （P27348） PENTAETHYLENE GLYCOL × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	BAIP2_HUMAN
Isoform	Q9UQB8-2
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–32； UniProt 335–366 Author chain F； PDBConstruct 1–32； UniProt 335–366 Author chain I； PDBConstruct 1–32； UniProt 335–366 Author chain L； PDBConstruct 1–32； UniProt 335–366

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	6bqt
Deposition date deposition_date	2017-11-28
Structure title title	Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and T360
Keywords keywords	phosphate binding protein, protein complex, cytoskeleton regulation, cell motility, SIGNALING PROTEIN; SIGNALING 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.

6bqt__assembly_2__model_1

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

Download this curve (.dat)

6bqt__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6bqt__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	27.18 Å
Rg (electron density)	26.28 Å
Total Rg	27.05 Å
Atom count	7783
Residues	476
Excluded volume	69405 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6bqt__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`6bqt__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`6bqt__assembly_3__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`6bqt__assembly_4__model_1`	trimeric （3）	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 (10)

Entity 1 Entity 1 polymer

Description description	14-3-3 protein theta
Molecular weight formula_weight	27795.2 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,D,E,G,H,J,K
Atom count atom_count	31276

MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIDNSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN

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 polymer

Description description	Insulin receptor substrate protein of 53 kDa, peptide (IRSp53)
Molecular weight formula_weight	3694.8 kDa
Source method src_method	syn
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,F,I,L

DSYSNTLPVRKSVTPKNSYATTENKTLPRSSS

Entity 3 Entity 3 non-polymer

Description description	2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
Molecular weight formula_weight	354.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	PENTAETHYLENE GLYCOL
Molecular weight formula_weight	238.3 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 5 Entity 5 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 non-polymer

Description description	TETRAETHYLENE GLYCOL
Molecular weight formula_weight	194.2 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 7 Entity 7 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 8 Entity 8 non-polymer

Description description	TRIETHYLENE GLYCOL
Molecular weight formula_weight	150.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 9 Entity 9 non-polymer

Description description	DI(HYDROXYETHYL)ETHER
Molecular weight formula_weight	106.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 10 Entity 10 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	93

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6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id	6bqtA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	20 — 14-3-3 domain

Domain ID domain_id	6bqtB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	20 — 14-3-3 domain

Domain ID domain_id	6bqtD00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	20 — 14-3-3 domain

Domain ID domain_id	6bqtE00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	20 — 14-3-3 domain

Domain ID domain_id	6bqtG00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	20 — 14-3-3 domain

Domain ID domain_id	6bqtH00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	20 — 14-3-3 domain

Domain ID domain_id	6bqtJ00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	20 — 14-3-3 domain

Domain ID domain_id	6bqtK00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	20 — 14-3-3 domain

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Unit-cell length a length_a	61.103 Å
Unit-cell length b length_b	69.572 Å
Unit-cell length c length_c	150.473 Å
Unit-cell angle α angle_alpha	99.16 °
Unit-cell angle β angle_beta	92.98 °
Unit-cell angle γ angle_gamma	115.98 °
Molecules per unit cell Z z_pdb	8

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

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	42.983 Å
R factor r_factor	0.2360
R_work r_work	0.2340
R_free r_free	0.2867

Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and T360

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

14-3-3 protein theta

State in the Current Structure

Other States of the Same Protein in the Database

Insulin receptor substrate protein of 53 kDa, peptide (IRSp53)

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

6bqt__assembly_2__model_1

6bqt__assembly_2__model_1 | I(q)

6bqt__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 (10)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 water

6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

7. Citations (1)

Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and T360

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

14-3-3 protein theta

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Insulin receptor substrate protein of 53 kDa, peptide (IRSp53)

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

6bqt__assembly_2__model_1

6bqt__assembly_2__model_1 | I(q)

6bqt__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 (10)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 water

6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

7. Citations (1)