SAXSdb — 6q0u

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

Erbin

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	peptide × 1 1,2-ETHANEDIOL × 2 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	peptide × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ERBIN_HUMAN
Isoform	Q96RT1-2
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–94； UniProt 1280–1369 Author chain B； PDBConstruct 5–94； UniProt 1280–1369

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	6q0u
Deposition date deposition_date	2019-08-02
Structure title title	Structure of the Erbin PDZ variant E-6a with a high-affinity C-terminal peptide
Keywords keywords	peptide-phage display, protein engineering, PDZ domains, C-terminal peptide, 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.

6q0u__assembly_2__model_1

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

Download this curve (.dat)

6q0u__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6q0u__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	14.18 Å
Rg (electron density)	12.45 Å
Total Rg	13.90 Å
Atom count	779
Residues	100
Excluded volume	13829 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6q0u__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`6q0u__assembly_2__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 (4)

Entity 1 Entity 1 polymer

Description description	Erbin
Molecular weight formula_weight	10273.7 kDa
Mutation mutation	S1294R, S1296A, V1351I
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	1709

SGSMEIRVRVEKDPELGFRIAGGVGGRGNPFRPDDDGIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIEHGQAISLLKTFQNTVELIIVREV

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	peptide
Molecular weight formula_weight	917.0 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

YYESGWL

Entity 3 Entity 3 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 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	134

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Unit-cell length a length_a	34.590 Å
Unit-cell length b length_b	38.090 Å
Unit-cell length c length_c	38.450 Å
Unit-cell angle α angle_alpha	83.04 °
Unit-cell angle β angle_beta	74.99 °
Unit-cell angle γ angle_gamma	63.66 °
Molecules per unit cell Z z_pdb	2

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

Resolution resolution	1.890 Å
Low-resolution limit resolution_low	37.140 Å
R factor r_factor	0.1840
R_work r_work	0.1780
R_free r_free	0.2370

Structure of the Erbin PDZ variant E-6a with a high-affinity C-terminal peptide

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

Erbin

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

6q0u__assembly_2__model_1

6q0u__assembly_2__model_1 | I(q)

6q0u__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 (4)

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 water

7. Citations (1)

Structure of the Erbin PDZ variant E-6a with a high-affinity C-terminal peptide

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

Erbin

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

6q0u__assembly_2__model_1

6q0u__assembly_2__model_1 | I(q)

6q0u__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 (4)

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 water

7. Citations (1)