SAXSdb — 1uou

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

THYMIDINE PHOSPHORYLASE

HOMO SAPIENS

UniProt P19971

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	5-CHLORO-6-(1-(2-IMINOPYRROLIDINYL) METHYL) URACIL × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TYPH_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 6–402； UniProt 12–408 Author chain A； PDBConstruct 403–474； UniProt 411–482

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	1uou
Deposition date deposition_date	2003-09-23
Structure title title	Crystal structure of human thymidine phosphorylase in complex with a small molecule inhibitor
Keywords keywords	PHOSPHORYLASE, TRANSFERASE, GLYCOSYLTRANSFERASE, CHEMOTAXIS, ANGIOGENESIS; TRANSFERASE
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.

1uou__assembly_1__model_1

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

Download this curve (.dat)

1uou__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1uou__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	34.03 Å
Rg (electron density)	33.39 Å
Total Rg	33.75 Å
Atom count	6408
Residues	876
Excluded volume	114640 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1uou__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	THYMIDINE PHOSPHORYLASE
Molecular weight formula_weight	49195.4 kDa
EC 编号 ec_number	2.4.2.4
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	3288

GSPGIPPAPGDFSGEGSQGLPDPSPEPKQLPELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQLVDKHSTGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPLGRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGLARALCSGSPAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRAGEPLRLGVGAELLVDVGQRLRRGTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAPLPFAELVLPPQQ

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	5-CHLORO-6-(1-(2-IMINOPYRROLIDINYL) METHYL) URACIL
Molecular weight formula_weight	242.7 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	75

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1uoua1
Class class	a — All alpha proteins
Fold Fold fold	a.46 — Methionine synthase domain-like
Superfamily Superfamily superfamily	a.46.2 — Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain
Family Family family	a.46.2.1 — Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain

Domain ID domain_id	d1uoua2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.27 — Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain
Superfamily Superfamily superfamily	c.27.1 — Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain
Family Family family	c.27.1.1 — Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain

Domain ID domain_id	d1uoua3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.41 — alpha/beta-Hammerhead
Superfamily Superfamily superfamily	d.41.3 — Pyrimidine nucleoside phosphorylase C-terminal domain
Family Family family	d.41.3.1 — Pyrimidine nucleoside phosphorylase C-terminal domain

CATH v4.4 (3 domains)

Domain ID domain_id	1uouA01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	970 — Transferase, Pyrimidine Nucleoside Phosphorylase; Chain A, domain 3
Homologous superfamily homologous superfamily	10 — Transferase, Pyrimidine Nucleoside Phosphorylase; Chain C

Domain ID domain_id	1uouA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1030 — Pyrimidine Nucleoside Phosphorylase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain

Domain ID domain_id	1uouA03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1170 — Aldehyde Oxidoreductase; domain 3
Homologous superfamily homologous superfamily	30 — Pyrimidine nucleoside phosphorylase-like, C-terminal domain

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Unit-cell length a length_a	69.990 Å
Unit-cell length b length_b	66.090 Å
Unit-cell length c length_c	96.870 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	106.54 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.110 Å
Low-resolution limit resolution_low	91.290 Å
R factor r_factor	0.1920
R_work r_work	0.1880
R_free r_free	0.2580

Crystal structure of human thymidine phosphorylase in complex with a small molecule inhibitor

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

THYMIDINE PHOSPHORYLASE

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

1uou__assembly_1__model_1

1uou__assembly_1__model_1 | I(q)

1uou__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) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)

Crystal structure of human thymidine phosphorylase in complex with a small molecule inhibitor

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

THYMIDINE PHOSPHORYLASE

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

1uou__assembly_1__model_1

1uou__assembly_1__model_1 | I(q)

1uou__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) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)