SAXSdb — 5nc7

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

Protein enabled homolog

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	;ActA-derived 10-mer Ac-FPPPPTEDEL-NH2 with acetylated (Ac) and amidated (NH2) termini. Phe is substitued by Trp to increase affinity for crystallization ; × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	;ActA-derived 10-mer Ac-FPPPPTEDEL-NH2 with acetylated (Ac) and amidated (NH2) termini. Phe is substitued by Trp to increase affinity for crystallization ; × 2 water × 1	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	;ActA-derived 10-mer Ac-FPPPPTEDEL-NH2 with acetylated (Ac) and amidated (NH2) termini. Phe is substitued by Trp to increase affinity for crystallization ; × 2 water × 1	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 3	;ActA-derived 10-mer Ac-FPPPPTEDEL-NH2 with acetylated (Ac) and amidated (NH2) termini. Phe is substitued by Trp to increase affinity for crystallization ; × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ENAH_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–113； UniProt 1–111 Author chain B； PDBConstruct 3–113； UniProt 1–111 Author chain C； PDBConstruct 3–113； UniProt 1–111 Author chain D； PDBConstruct 3–113； UniProt 1–111

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	5nc7
Deposition date deposition_date	2017-03-03
Structure title title	ENAH EVH1 in complex with Ac-WPPPPTEDEL-NH2
Keywords keywords	proline-rich motif, ActA, protein-protein interaction, cell adhesion; CELL ADHESION
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.

5nc7__assembly_3__model_1

Assembly 3 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5nc7__assembly_3__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5nc7__assembly_3__model_1 | P(r) · Pending

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

Rg（Guinier）	15.27 Å
Rg (electron density)	13.88 Å
Total Rg	15.08 Å
Atom count	1018
Residues	128
Excluded volume	17872 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5nc7__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`5nc7__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`5nc7__assembly_3__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`5nc7__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 (3)

Entity 1 Entity 1 polymer

Description description	Protein enabled homolog
Molecular weight formula_weight	12628.3 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	3989

GSMSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVL

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-Gold(DE3)pLysS AG' ;

Entity 2 Entity 2 polymer

Description description	;ActA-derived 10-mer Ac-FPPPPTEDEL-NH2 with acetylated (Ac) and amidated (NH2) termini. Phe is substitued by Trp to increase affinity for crystallization ;
Molecular weight formula_weight	1204.3 kDa
Source method src_method	syn
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	K,I,J,L,Z,X,Y,W

XWPPPPTEDELX

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	4

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	5nc7A00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	29 — PH-domain like
Homologous superfamily homologous superfamily	30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Domain ID domain_id	5nc7B00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	29 — PH-domain like
Homologous superfamily homologous superfamily	30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Domain ID domain_id	5nc7C00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	29 — PH-domain like
Homologous superfamily homologous superfamily	30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Domain ID domain_id	5nc7D00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	29 — PH-domain like
Homologous superfamily homologous superfamily	30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

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Unit-cell length a length_a	187.960 Å
Unit-cell length b length_b	34.430 Å
Unit-cell length c length_c	110.990 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.53 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	32

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	48.337 Å
R factor r_factor	0.2123
R_work r_work	0.2093
R_free r_free	0.2720

ENAH EVH1 in complex with Ac-WPPPPTEDEL-NH2

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

Protein enabled homolog

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

5nc7__assembly_3__model_1

5nc7__assembly_3__model_1 | I(q)

5nc7__assembly_3__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (2)

ENAH EVH1 in complex with Ac-WPPPPTEDEL-NH2

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

Protein enabled homolog

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

5nc7__assembly_3__model_1

5nc7__assembly_3__model_1 | I(q)

5nc7__assembly_3__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (2)