SAXSdb — 1fsi

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

CYCLIC PHOSPHODIESTERASE

Arabidopsis thaliana

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	SULFATE ION × 3 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	SULFATE ION × 3 water × 1	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	SULFATE ION × 3 water × 1	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 6	SULFATE ION × 18 water × 6	Consistent with protein count
5	Protein homooligomer	Homooligomer	Protein 2	SULFATE ION × 6 water × 2	Consistent with protein count
6	Protein homooligomer	Homooligomer	Protein 2	SULFATE ION × 6 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CPD_ARATH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–181； UniProt 1–181 Author chain B； PDBConstruct 1–181； UniProt 1–181 Author chain C； PDBConstruct 1–181； UniProt 1–181

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	1fsi
Deposition date deposition_date	2000-09-10
Structure title title	CRYSTAL STRUCTURE OF CYCLIC NUCLEOTIDE PHOSPHODIESTERASE OF APPR>P FROM ARABIDOPSIS THALIANA
Keywords keywords	;ADP-ribose 1'', 2''-cyclic phosphate, Appr>p, 2', 3'-cyclic nucleotide phosphodiesterase, 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.

1fsi__assembly_1__model_1

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

Download this curve (.dat)

1fsi__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1fsi__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	18.22 Å
Rg (electron density)	17.02 Å
Total Rg	18.10 Å
Atom count	1434
Residues	179
Excluded volume	25431 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1fsi__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1fsi__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1fsi__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1fsi__assembly_4__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`1fsi__assembly_5__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`1fsi__assembly_6__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	CYCLIC PHOSPHODIESTERASE
Molecular weight formula_weight	21510.3 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	4413

MEEVKKDVYSVWALPDEESEPRFKKLMEALRSEFTGPRFVPHVTVAVSAYLTADEAKKMFESACDGLKAYTATVDRVSTGTFFFQCVFLLLQTTPEVMEAGEHCKNHFNCSTTTPYMPHLSLLYAELTEEEKKNAQEKAYTLDSSLDGLSFRLNRLALCKTDTEDKTLETWETVAVCNLNPGSHHHHHH

Source Source

Source organism organism	Arabidopsis thaliana
Common name common_name	thale cress
NCBI taxonomy ID ncbi_taxonomy_id	3702
Host organism host_organism	Escherichia coli BL21(DE3)

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	9

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	229

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6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1fsia1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.61 — LigT-like
Superfamily Superfamily superfamily	d.61.1 — LigT-like
Family Family family	d.61.1.1 — tRNA splicing product Appr>p cyclic nucleotide phosphodiesterase

Domain ID domain_id	d1fsia2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1fsib_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.61 — LigT-like
Superfamily Superfamily superfamily	d.61.1 — LigT-like
Family Family family	d.61.1.1 — tRNA splicing product Appr>p cyclic nucleotide phosphodiesterase

Domain ID domain_id	d1fsic_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.61 — LigT-like
Superfamily Superfamily superfamily	d.61.1 — LigT-like
Family Family family	d.61.1.1 — tRNA splicing product Appr>p cyclic nucleotide phosphodiesterase

CATH v4.4 (3 domains)

Domain ID domain_id	1fsiA00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1140 — Cyclic Phosphodiesterase; Chain: A,
Homologous superfamily homologous superfamily	10 — Cyclic phosphodiesterase

Domain ID domain_id	1fsiB00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1140 — Cyclic Phosphodiesterase; Chain: A,
Homologous superfamily homologous superfamily	10 — Cyclic phosphodiesterase

Domain ID domain_id	1fsiC00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1140 — Cyclic Phosphodiesterase; Chain: A,
Homologous superfamily homologous superfamily	10 — Cyclic phosphodiesterase

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Unit-cell length a length_a	125.916 Å
Unit-cell length b length_b	125.916 Å
Unit-cell length c length_c	209.897 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	36

Space group space_group	P 61 2 2
Space-group number int_tables_number	178
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	19.910 Å
R factor r_factor	0.1960
R_work r_work	0.1960
R_free r_free	0.2650

CRYSTAL STRUCTURE OF CYCLIC NUCLEOTIDE PHOSPHODIESTERASE OF APPR>P FROM ARABIDOPSIS THALIANA

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

CYCLIC PHOSPHODIESTERASE

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

1fsi__assembly_1__model_1

1fsi__assembly_1__model_1 | I(q)

1fsi__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

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) 7 domains

SCOP 2.08 (4 domains)

CATH v4.4 (3 domains)

7. Citations (2)

CRYSTAL STRUCTURE OF CYCLIC NUCLEOTIDE PHOSPHODIESTERASE OF APPR>P FROM ARABIDOPSIS THALIANA

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

CYCLIC PHOSPHODIESTERASE

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

1fsi__assembly_1__model_1

1fsi__assembly_1__model_1 | I(q)

1fsi__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

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) 7 domains

SCOP 2.08 (4 domains)

CATH v4.4 (3 domains)

7. Citations (2)