1f3y

SOLUTION STRUCTURE OF THE NUDIX ENZYME DIADENOSINE TETRAPHOSPHATE HYDROLASE FROM LUPINUS ANGUSTIFOLIUS L.

Method: SOLUTION NMR

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

;DIADENOSINE 5',5'''-P1,P4-TETRAPHOSPHATE HYDROLASE ;

Lupinus angustifolius

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O04841_LUPAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–165； UniProt 35–199

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	1f3y
Deposition date deposition_date	2000-06-06
Structure title title	SOLUTION STRUCTURE OF THE NUDIX ENZYME DIADENOSINE TETRAPHOSPHATE HYDROLASE FROM LUPINUS ANGUSTIFOLIUS L.
Keywords keywords	Enzyme, MIXED 4-STRANDED BETA SHEET, 2-STRANDED ANTIPARALLEL SHEET, ALPHA-BETA-ALPHA SANDWICH, HYDROLASE; HYDROLASE
Experimental Method method	SOLUTION NMR

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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.

1f3y__assembly_1__model_12

Assembly 1 · Model 12 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1f3y__assembly_1__model_12 | I(q)

100 plotted points; both axes use logarithmic scales.

1f3y__assembly_1__model_12 | P(r) · Pending

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

Rg（Guinier）	16.89 Å
Rg (electron density)	15.51 Å
Total Rg	16.67 Å
Atom count	2617
Residues	165
Excluded volume	23615 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1f3y__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	2	`1f3y__assembly_1__model_2`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	3	`1f3y__assembly_1__model_3`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	4	`1f3y__assembly_1__model_4`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	5	`1f3y__assembly_1__model_5`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	6	`1f3y__assembly_1__model_6`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	7	`1f3y__assembly_1__model_7`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	8	`1f3y__assembly_1__model_8`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	9	`1f3y__assembly_1__model_9`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	10	`1f3y__assembly_1__model_10`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	11	`1f3y__assembly_1__model_11`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	12	`1f3y__assembly_1__model_12`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	13	`1f3y__assembly_1__model_13`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	14	`1f3y__assembly_1__model_14`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	15	`1f3y__assembly_1__model_15`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	16	`1f3y__assembly_1__model_16`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	17	`1f3y__assembly_1__model_17`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	18	`1f3y__assembly_1__model_18`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	19	`1f3y__assembly_1__model_19`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	20	`1f3y__assembly_1__model_20`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	21	`1f3y__assembly_1__model_21`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	22	`1f3y__assembly_1__model_22`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	23	`1f3y__assembly_1__model_23`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	24	`1f3y__assembly_1__model_24`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	25	`1f3y__assembly_1__model_25`	monomeric （1）	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 (1)

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1f3ya_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.113 — Nudix
Superfamily Superfamily superfamily	d.113.1 — Nudix
Family Family family	d.113.1.1 — MutT-like

CATH v4.4 (1 domains)

Domain ID domain_id	1f3yA00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	79 — Nucleoside Triphosphate Pyrophosphohydrolase
Homologous superfamily homologous superfamily	10 — Nucleoside Triphosphate Pyrophosphohydrolase

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

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

Description description	;DIADENOSINE 5',5'''-P1,P4-TETRAPHOSPHATE HYDROLASE ;
Molecular weight formula_weight	18834.2 kDa
EC 编号 ec_number	3.6.1.17
Mutation mutation	Y1G/C2P/H3L/S4G
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	65425

Source organism organism	Lupinus angustifolius
Common name common_name	narrow-leaved blue lupine
NCBI taxonomy ID ncbi_taxonomy_id	3871
Host organism host_organism	Escherichia coli

SOLUTION STRUCTURE OF THE NUDIX ENZYME DIADENOSINE TETRAPHOSPHATE HYDROLASE FROM LUPINUS ANGUSTIFOLIUS L.

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

;DIADENOSINE 5',5'''-P1,P4-TETRAPHOSPHATE HYDROLASE ;

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

1f3y__assembly_1__model_12

1f3y__assembly_1__model_12 | I(q)

1f3y__assembly_1__model_12 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)

SOLUTION STRUCTURE OF THE NUDIX ENZYME DIADENOSINE TETRAPHOSPHATE HYDROLASE FROM LUPINUS ANGUSTIFOLIUS L.

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

;DIADENOSINE 5',5'''-P1,P4-TETRAPHOSPHATE HYDROLASE ;

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

1f3y__assembly_1__model_12

1f3y__assembly_1__model_12 | I(q)

1f3y__assembly_1__model_12 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)