3cae

Structure of NNQQNY as an insert in T7 endonuclease I

Method: X-RAY DIFFRACTION

▼

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

Endonuclease I

Enterobacteria phage T7

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 10	water × 8	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ENDO_BPT7
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–27； UniProt 18–43 Author chain A； PDBConstruct 37–132； UniProt 50–145 Author chain B； PDBConstruct 2–27； UniProt 18–43 Author chain B； PDBConstruct 37–132； UniProt 50–145 Author chain C； PDBConstruct 2–27； UniProt 18–43 Author chain C； PDBConstruct 37–132； UniProt 50–145 Author chain D； PDBConstruct 2–27； UniProt 18–43 Author chain D； PDBConstruct 37–132； UniProt 50–145 Author chain E； PDBConstruct 2–27； UniProt 18–43 Author chain E； PDBConstruct 37–132； UniProt 50–145 Author chain F； PDBConstruct 2–27； UniProt 18–43 Author chain F； PDBConstruct 37–132； UniProt 50–145 Author chain G； PDBConstruct 2–27； UniProt 18–43 Author chain G； PDBConstruct 37–132； UniProt 50–145 Author chain H； PDBConstruct 2–27； UniProt 18–43 Author chain H； PDBConstruct 37–132； UniProt 50–145 Author chain I； PDBConstruct 2–27； UniProt 18–43 Author chain I； PDBConstruct 37–132； UniProt 50–145 Author chain J； PDBConstruct 2–27； UniProt 18–43 Author chain J； PDBConstruct 37–132； UniProt 50–145

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	3cae
Deposition date deposition_date	2008-02-19
Structure title title	Structure of NNQQNY as an insert in T7 endonuclease I
Keywords keywords	T7 endonuclease I, amyloid, steric zipper, Hydrolase; HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

▼

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.

3cae__assembly_1__model_1

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

Download this curve (.dat)

3cae__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3cae__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	35.85 Å
Rg (electron density)	35.22 Å
Total Rg	35.97 Å
Atom count	11060
Residues	1320
Excluded volume	197590 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3cae__assembly_1__model_1`	decameric （10）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (2)

▼

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

Domain ID domain_id	d3caea_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.52 — Restriction endonuclease-like
Superfamily Superfamily superfamily	c.52.1 — Restriction endonuclease-like
Family Family family	c.52.1.17 — Endonuclease I (Holliday junction resolvase)

Domain ID domain_id	d3caeb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.52 — Restriction endonuclease-like
Superfamily Superfamily superfamily	c.52.1 — Restriction endonuclease-like
Family Family family	c.52.1.17 — Endonuclease I (Holliday junction resolvase)

Domain ID domain_id	d3caec_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.52 — Restriction endonuclease-like
Superfamily Superfamily superfamily	c.52.1 — Restriction endonuclease-like
Family Family family	c.52.1.17 — Endonuclease I (Holliday junction resolvase)

Domain ID domain_id	d3caed_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.52 — Restriction endonuclease-like
Superfamily Superfamily superfamily	c.52.1 — Restriction endonuclease-like
Family Family family	c.52.1.17 — Endonuclease I (Holliday junction resolvase)

Domain ID domain_id	d3caee_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.52 — Restriction endonuclease-like
Superfamily Superfamily superfamily	c.52.1 — Restriction endonuclease-like
Family Family family	c.52.1.17 — Endonuclease I (Holliday junction resolvase)

Domain ID domain_id	d3caef_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.52 — Restriction endonuclease-like
Superfamily Superfamily superfamily	c.52.1 — Restriction endonuclease-like
Family Family family	c.52.1.17 — Endonuclease I (Holliday junction resolvase)

Domain ID domain_id	d3caeg_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.52 — Restriction endonuclease-like
Superfamily Superfamily superfamily	c.52.1 — Restriction endonuclease-like
Family Family family	c.52.1.17 — Endonuclease I (Holliday junction resolvase)

Domain ID domain_id	d3caeh_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.52 — Restriction endonuclease-like
Superfamily Superfamily superfamily	c.52.1 — Restriction endonuclease-like
Family Family family	c.52.1.17 — Endonuclease I (Holliday junction resolvase)

Domain ID domain_id	d3caei_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.52 — Restriction endonuclease-like
Superfamily Superfamily superfamily	c.52.1 — Restriction endonuclease-like
Family Family family	c.52.1.17 — Endonuclease I (Holliday junction resolvase)

Domain ID domain_id	d3caej_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.52 — Restriction endonuclease-like
Superfamily Superfamily superfamily	c.52.1 — Restriction endonuclease-like
Family Family family	c.52.1.17 — Endonuclease I (Holliday junction resolvase)

CATH v4.4 (10 domains)

Domain ID domain_id	3caeA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	91 — Restriction Endonuclease
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3caeB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	91 — Restriction Endonuclease
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3caeC00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	91 — Restriction Endonuclease
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3caeD00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	91 — Restriction Endonuclease
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3caeE00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	91 — Restriction Endonuclease
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3caeF00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	91 — Restriction Endonuclease
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3caeG00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	91 — Restriction Endonuclease
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3caeH00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	91 — Restriction Endonuclease
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3caeI00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	91 — Restriction Endonuclease
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3caeJ00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	91 — Restriction Endonuclease
Homologous superfamily homologous superfamily	30 —

▶

Unit-cell length a length_a	88.408 Å
Unit-cell length b length_b	140.343 Å
Unit-cell length c length_c	88.508 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	93.37 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	20

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

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	90.000 Å
R factor r_factor	—
R_work r_work	0.2405
R_free r_free	0.2840

Description description	Endonuclease I
Molecular weight formula_weight	15650.8 kDa
EC 编号 ec_number	3.1.21.2
Source method src_method	man
Copy count entity_count	10

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J
Atom count atom_count	11075

Structure of NNQQNY as an insert in T7 endonuclease I

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

Endonuclease I

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

3cae__assembly_1__model_1

3cae__assembly_1__model_1 | I(q)

3cae__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

CATH v4.4 (10 domains)

7. Citations (1)

Source organism organism	Enterobacteria phage T7
NCBI taxonomy ID ncbi_taxonomy_id	10760
Host organism host_organism	Escherichia coli BL21(DE3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	15

Structure of NNQQNY as an insert in T7 endonuclease I

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

Endonuclease I

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

3cae__assembly_1__model_1

3cae__assembly_1__model_1 | I(q)

3cae__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

CATH v4.4 (10 domains)

7. Citations (1)