1o17

ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD)

Method: X-RAY DIFFRACTION

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

ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE

Sulfolobus solfataricus

State in the Current Structure

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TRPD_SULSO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–345； UniProt 1–345 Author chain B； PDBConstruct 1–345； UniProt 1–345 Author chain C； PDBConstruct 1–345； UniProt 1–345 Author chain D； PDBConstruct 1–345； UniProt 1–345

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	1o17
Deposition date deposition_date	2002-10-29
Structure title title	ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD)
Keywords keywords	nucleoside-phosphorylases, TRANSFERASE; 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.

1o17__assembly_1__model_1

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

Download this curve (.dat)

1o17__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1o17__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	33.82 Å
Rg (electron density)	33.77 Å
Total Rg	33.99 Å
Atom count	5255
Residues	684
Excluded volume	95184 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1o17__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1o17__assembly_2__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 (2)

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6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d1o17a1
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	d1o17a2
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	d1o17b1
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	d1o17b2
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	d1o17c1
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	d1o17c2
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	d1o17d1
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	d1o17d2
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

CATH v4.4 (8 domains)

Domain ID domain_id	1o17A01
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	1o17A02
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	1o17B01
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	1o17B02
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	1o17C01
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	1o17C02
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	1o17D01
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	1o17D02
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

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Unit-cell length a length_a	92.340 Å
Unit-cell length b length_b	65.850 Å
Unit-cell length c length_c	116.440 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	107.56 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 2 1
Space-group number int_tables_number	3
Crystal system crystal_system	—

Resolution resolution	2.050 Å
Low-resolution limit resolution_low	18.000 Å
R factor r_factor	—
R_work r_work	0.2130
R_free r_free	0.2600

Description description	ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE
Molecular weight formula_weight	37619.5 kDa
EC 编号 ec_number	2.4.2.18
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	11430

ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD)

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

ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE

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

1o17__assembly_1__model_1

1o17__assembly_1__model_1 | I(q)

1o17__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (2)

Source organism organism	Sulfolobus solfataricus
NCBI taxonomy ID ncbi_taxonomy_id	2287
Host organism host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	935

ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD)

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

ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE

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

1o17__assembly_1__model_1

1o17__assembly_1__model_1 | I(q)

1o17__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (2)