SAXSdb — 1ln0

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

intron-associated endonuclease 1

Enterobacteria phage T4

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	SULFATE ION × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TEV1_BPT4
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–97； UniProt 1–97 Author chain B； PDBConstruct 1–97； UniProt 1–97

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	1ln0
Deposition date deposition_date	2002-05-02
Structure title title	Structure of the Catalytic Domain of Homing Endonuclease I-TevI
Keywords keywords	alpha/beta fold, HYDROLASE; HYDROLASE
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.

1ln0__assembly_1__model_1

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

Download this curve (.dat)

1ln0__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1ln0__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	19.55 Å
Rg (electron density)	18.86 Å
Total Rg	19.71 Å
Atom count	1555
Residues	186
Excluded volume	27655 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1ln0__assembly_1__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	intron-associated endonuclease 1
Molecular weight formula_weight	11378.0 kDa
EC 编号 ec_number	3.1.-.-
Mutation mutation	R27A
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	1797

MKSGIYQIKNTLNNKVYVGSAKDFEKAWKRHFKDLEKGCHSSIKLQRSFNKHGNVFECSILEEIPYEKDLIIERENFWIKELNSKINGYNIADATFG

Source Source

Source organism organism	Enterobacteria phage T4
NCBI taxonomy ID ncbi_taxonomy_id	10665
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	208

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1ln0a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.226 — GIY-YIG endonuclease
Superfamily Superfamily superfamily	d.226.1 — GIY-YIG endonuclease
Family Family family	d.226.1.1 — GIY-YIG endonuclease

Domain ID domain_id	d1ln0b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.226 — GIY-YIG endonuclease
Superfamily Superfamily superfamily	d.226.1 — GIY-YIG endonuclease
Family Family family	d.226.1.1 — GIY-YIG endonuclease

CATH v4.4 (2 domains)

Domain ID domain_id	1ln0A00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1440 — GIY-YIG endonuclease
Homologous superfamily homologous superfamily	10 — GIY-YIG endonuclease

Domain ID domain_id	1ln0B00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1440 — GIY-YIG endonuclease
Homologous superfamily homologous superfamily	10 — GIY-YIG endonuclease

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Unit-cell length a length_a	123.870 Å
Unit-cell length b length_b	56.580 Å
Unit-cell length c length_c	35.450 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.2020
R_work r_work	0.2020
R_free r_free	0.2550

Structure of the Catalytic Domain of Homing Endonuclease I-TevI

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

intron-associated endonuclease 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

1ln0__assembly_1__model_1

1ln0__assembly_1__model_1 | I(q)

1ln0__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 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Structure of the Catalytic Domain of Homing Endonuclease I-TevI

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

intron-associated endonuclease 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

1ln0__assembly_1__model_1

1ln0__assembly_1__model_1 | I(q)

1ln0__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 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)