SAXSdb — 4hop

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

Alpha-1-syntrophin

Mus musculus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Nitric oxide synthase, brain × 1 （P29476） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Nitric oxide synthase, brain × 1 （P29476） water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Nitric oxide synthase, brain × 1 （P29476） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SNTA1_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–88； UniProt 77–162 Author chain C； PDBConstruct 3–88； UniProt 77–162 Author chain E； PDBConstruct 3–88； UniProt 77–162

Nitric oxide synthase, brain

Rattus norvegicus

UniProt P29476

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Alpha-1-syntrophin × 1 （Q61234） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Alpha-1-syntrophin × 1 （Q61234） water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Alpha-1-syntrophin × 1 （Q61234） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	NOS1_RAT
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–123； UniProt 4–126 Author chain D； PDBConstruct 1–123； UniProt 4–126 Author chain F； PDBConstruct 1–123； UniProt 4–126

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	4hop
Deposition date deposition_date	2012-10-22
Structure title title	Crystal structure of the computationally designed NNOS-Syntrophin complex
Keywords keywords	PDZ, Protein Binding, Dimerization, Mutation, Membrane, MEMBRANE PROTEIN-OXIDOREDUCTASE complex; MEMBRANE PROTEIN/OXIDOREDUCTASE
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.

4hop__assembly_1__model_1

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

Download this curve (.dat)

4hop__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4hop__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	20.52 Å
Rg (electron density)	19.70 Å
Total Rg	20.56 Å
Atom count	1556
Residues	207
Excluded volume	28100 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4hop__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`4hop__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`4hop__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 (3)

Entity 1 Entity 1 polymer

Description description	Alpha-1-syntrophin
Molecular weight formula_weight	9389.8 kDa
Mutation mutation	H142F
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E
Atom count atom_count	5203

GSLQRRRVTVRKADAGGLGISIKGGRENKMPILISKIFKGLAADQTEALFVGDAILSVNGEDLSSATFDEAVQALKKTGKEVVLEVKY

Source Source

Source organism organism	Mus musculus
Common name common_name	mouse
NCBI taxonomy ID ncbi_taxonomy_id	10090
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Nitric oxide synthase, brain
Molecular weight formula_weight	13289.4 kDa
EC 编号 ec_number	1.14.13.39
Mutation mutation	T109M
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F

NTFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQAGDIILAVNDRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLEMTFTGDGTPKTIRVTQPL

Source Source

Source organism organism	Rattus norvegicus
Common name common_name	brown rat,rat,rats
NCBI taxonomy ID ncbi_taxonomy_id	10116
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	501

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6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id	4hopA00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	42 — Pdz3 Domain
Homologous superfamily homologous superfamily	10 — PDZ domain

Domain ID domain_id	4hopB00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	42 — Pdz3 Domain
Homologous superfamily homologous superfamily	10 — PDZ domain

Domain ID domain_id	4hopC00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	42 — Pdz3 Domain
Homologous superfamily homologous superfamily	10 — PDZ domain

Domain ID domain_id	4hopD00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	42 — Pdz3 Domain
Homologous superfamily homologous superfamily	10 — PDZ domain

Domain ID domain_id	4hopE00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	42 — Pdz3 Domain
Homologous superfamily homologous superfamily	10 — PDZ domain

Domain ID domain_id	4hopF00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	42 — Pdz3 Domain
Homologous superfamily homologous superfamily	10 — PDZ domain

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Unit-cell length a length_a	61.196 Å
Unit-cell length b length_b	102.503 Å
Unit-cell length c length_c	64.100 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	118.61 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	6

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

Resolution resolution	2.290 Å
Low-resolution limit resolution_low	47.570 Å
R factor r_factor	0.2260
R_work r_work	0.2230
R_free r_free	0.2730

Crystal structure of the computationally designed NNOS-Syntrophin complex

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

Alpha-1-syntrophin

State in the Current Structure

Other States of the Same Protein in the Database

Nitric oxide synthase, brain

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

4hop__assembly_1__model_1

4hop__assembly_1__model_1 | I(q)

4hop__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (1)

Crystal structure of the computationally designed NNOS-Syntrophin complex

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

Alpha-1-syntrophin

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Nitric oxide synthase, brain

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

4hop__assembly_1__model_1

4hop__assembly_1__model_1 | I(q)

4hop__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (1)