SAXSdb — 9frp

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

Protein mono-ADP-ribosyltransferase PARP10

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	;4-[[4-fluoranyl-3-[[(5~{S})-5-methyl-3-(1,3-thiazol-2-yl)-6,8-dihydro-5~{H}-[1,2,4]triazolo[4,3-a]pyrazin-7-yl]carbonyl]phenyl]methyl]-2~{H}-phthalazin-1-one ; × 1 CHLORIDE ION × 3 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	;4-[[4-fluoranyl-3-[[(5~{S})-5-methyl-3-(1,3-thiazol-2-yl)-6,8-dihydro-5~{H}-[1,2,4]triazolo[4,3-a]pyrazin-7-yl]carbonyl]phenyl]methyl]-2~{H}-phthalazin-1-one ; × 1 CHLORIDE ION × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PAR10_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–194； UniProt 814–1006 Author chain B； PDBConstruct 2–194； UniProt 814–1006

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	9frp
Deposition date deposition_date	2024-06-19
Last revision last_revision	2026-01-14
Structure title title	Human PARP10 ART domain bound to a phthalazinone-based inhibitor.
Keywords keywords	mono-ADP-ribosyltransferase, PARP10, kinase regulation, NUCLEAR PROTEIN; NUCLEAR PROTEIN
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.

9frp__assembly_1__model_1

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

Download this curve (.dat)

9frp__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9frp__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	17.93 Å
Rg (electron density)	16.71 Å
Total Rg	17.83 Å
Atom count	1570
Residues	192
Excluded volume	27399 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9frp__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`9frp__assembly_2__model_1`	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 (4)

Entity 1 Entity 1 polymer

Description description	Protein mono-ADP-ribosyltransferase PARP10
Molecular weight formula_weight	22483.5 kDa
EC 编号 ec_number	2.4.2.-
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	3881

MKGPWNNLERLAENTGEFQEVVRAFYDTLDAARSSIRVVRVERVSHPLLQQQYELYRERLLQRCERRPVEQVLYHGTTAPAVPDICAHGFNRSFCGRNATVYGKGVYFAKRASLSVQDRYSPPNADGHKAVFVARVLTGDYGQGRRGLRAPPLRGPGHVLLRYDSAVDCICQPSIFVIFHDTQALPTHLITCEHAHHH

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	;4-[[4-fluoranyl-3-[[(5~{S})-5-methyl-3-(1,3-thiazol-2-yl)-6,8-dihydro-5~{H}-[1,2,4]triazolo[4,3-a]pyrazin-7-yl]carbonyl]phenyl]methyl]-2~{H}-phthalazin-1-one ;
Molecular weight formula_weight	501.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	539

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Unit-cell length a length_a	51.752 Å
Unit-cell length b length_b	88.121 Å
Unit-cell length c length_c	57.574 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	104.38 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	1.400 Å
Low-resolution limit resolution_low	47.170 Å
R factor r_factor	0.1556
R_work r_work	0.1546
R_free r_free	0.1750

Human PARP10 ART domain bound to a phthalazinone-based inhibitor.

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

Protein mono-ADP-ribosyltransferase PARP10

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

9frp__assembly_1__model_1

9frp__assembly_1__model_1 | I(q)

9frp__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Citations (1)

Human PARP10 ART domain bound to a phthalazinone-based inhibitor.

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

Protein mono-ADP-ribosyltransferase PARP10

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

9frp__assembly_1__model_1

9frp__assembly_1__model_1 | I(q)

9frp__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Citations (1)