SAXSdb — 3tq7

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

Microtubule-associated protein RP/EB family member 1

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Microtubule-associated protein RP/EB family member 3 × 1 （Q9UPY8） Dynactin subunit 1 × 2 （Q14203） water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MARE1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–78； UniProt 191–268

Microtubule-associated protein RP/EB family member 3

Homo sapiens

UniProt Q9UPY8

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Microtubule-associated protein RP/EB family member 1 × 1 （Q15691） Dynactin subunit 1 × 2 （Q14203） water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MARE3_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–82； UniProt 200–281

Dynactin subunit 1

Homo sapiens

UniProt Q14203

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Microtubule-associated protein RP/EB family member 1 × 1 （Q15691） Microtubule-associated protein RP/EB family member 3 × 1 （Q9UPY8） water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	DCTN1_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain P； PDBConstruct 1–71； UniProt 27–97 Author chain Q； PDBConstruct 1–71； UniProt 27–97

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	3tq7
Deposition date deposition_date	2011-09-09
Structure title title	EB1c/EB3c heterodimer in complex with the CAP-Gly domain of P150glued
Keywords keywords	CAP-Gly domain, protein-protein interaction, microtubule binding, cytoskeleton, PROTEIN BINDING; PROTEIN BINDING
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.

3tq7__assembly_1__model_1

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

Download this curve (.dat)

3tq7__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3tq7__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	23.52 Å
Rg (electron density)	22.60 Å
Total Rg	23.48 Å
Atom count	2016
Residues	252
Excluded volume	35961 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3tq7__assembly_1__model_1`	tetrameric （4）	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 (4)

Entity 1 Entity 1 polymer

Description description	Microtubule-associated protein RP/EB family member 1
Molecular weight formula_weight	9067.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2057

DEAAELMQQVNVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRIVDILYATDEGFVIPDEGGPQEEQEEY

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

Entity 2 Entity 2 polymer

Description description	Microtubule-associated protein RP/EB family member 3
Molecular weight formula_weight	9517.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

AQILELNQQLVDLKLTVDGLEKERDFYFSKLRDIELICQEHESENSPVISGIIGILYATEEGFAPPEDDEIEEHQQEDQDEY

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

Entity 3 Entity 3 polymer

Description description	Dynactin subunit 1
Molecular weight formula_weight	7781.9 kDa
Mutation mutation	A49M
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	P,Q

LRVGSRVEVIGKGHRGTVAYVGMTLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVF

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

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	36

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3tq7a_
Class class	a — All alpha proteins
Fold Fold fold	a.245 — EB1 dimerisation domain-like
Superfamily Superfamily superfamily	a.245.1 — EB1 dimerisation domain-like
Family Family family	a.245.1.1 — EB1 dimerisation domain-like

Domain ID domain_id	d3tq7b_
Class class	a — All alpha proteins
Fold Fold fold	a.245 — EB1 dimerisation domain-like
Superfamily Superfamily superfamily	a.245.1 — EB1 dimerisation domain-like
Family Family family	a.245.1.1 — EB1 dimerisation domain-like

Domain ID domain_id	d3tq7p_
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.10 — Cap-Gly domain
Family Family family	b.34.10.1 — Cap-Gly domain

Domain ID domain_id	d3tq7q_
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.10 — Cap-Gly domain
Family Family family	b.34.10.1 — Cap-Gly domain

CATH v4.4 (4 domains)

Domain ID domain_id	3tq7A00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	1430 —

Domain ID domain_id	3tq7B00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	1430 —

Domain ID domain_id	3tq7P00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	190 — CAP Gly-rich-like domain

Domain ID domain_id	3tq7Q00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	190 — CAP Gly-rich-like domain

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Unit-cell length a length_a	41.150 Å
Unit-cell length b length_b	103.560 Å
Unit-cell length c length_c	48.130 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	113.64 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	44.090 Å
R factor r_factor	0.2290
R_work r_work	0.2255
R_free r_free	0.2811

EB1c/EB3c heterodimer in complex with the CAP-Gly domain of P150glued

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

Microtubule-associated protein RP/EB family member 1

State in the Current Structure

Other States of the Same Protein in the Database

Microtubule-associated protein RP/EB family member 3

State in the Current Structure

Other States of the Same Protein in the Database

Dynactin subunit 1

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

3tq7__assembly_1__model_1

3tq7__assembly_1__model_1 | I(q)

3tq7__assembly_1__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

EB1c/EB3c heterodimer in complex with the CAP-Gly domain of P150glued

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

Microtubule-associated protein RP/EB family member 1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Microtubule-associated protein RP/EB family member 3

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Dynactin subunit 1

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

3tq7__assembly_1__model_1

3tq7__assembly_1__model_1 | I(q)

3tq7__assembly_1__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)