1usy

ATP phosphoribosyl transferase (HisG:HisZ) complex from Thermotoga maritima

Method: X-RAY DIFFRACTION

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

ATP PHOSPHORIBOSYLTRANSFERASE REGULATORY SUBUNIT

THERMOTOGA MARITIMA

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 8	ATP PHOSPHORIBOSYLTRANSFERASE × 3 （Q9X0D2） ATP PHOSPHORIBOSYLTRANSFERASE × 1 （Q9X0D2） HISTIDINE × 8 PHOSPHATE ION × 6 water × 8	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HISZ_THEMA
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–275； UniProt 1–275 Author chain B； PDBConstruct 1–275； UniProt 1–275 Author chain D； PDBConstruct 1–275； UniProt 1–275 Author chain C； PDBConstruct 1–275； UniProt 1–275

ATP PHOSPHORIBOSYLTRANSFERASE

THERMOTOGA MARITIMA

UniProt Q9X0D2

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 8	ATP PHOSPHORIBOSYLTRANSFERASE REGULATORY SUBUNIT × 3 （Q9X0D3） ATP PHOSPHORIBOSYLTRANSFERASE REGULATORY SUBUNIT × 1 （Q9X0D3） HISTIDINE × 8 PHOSPHATE ION × 6 water × 8	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HIS1_THEMA
Isoform	—
PDB entities	3, 4
Chains and sequence ranges	Author chain E； PDBConstruct 1–208； UniProt 1–208 Author chain F； PDBConstruct 1–208； UniProt 1–208 Author chain G； PDBConstruct 1–208； UniProt 1–208 Author chain H； PDBConstruct 1–208； UniProt 1–208

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	1usy
Deposition date deposition_date	2003-12-01
Structure title title	ATP phosphoribosyl transferase (HisG:HisZ) complex from Thermotoga maritima
Keywords keywords	TRANSFERASE, ATP PHOSPHORIBOSYL TRANSFERASE, AMINOACYL-TRNA SYNTHETASE; 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.

1usy__assembly_1__model_1

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

Download this curve (.dat)

1usy__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1usy__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	40.69 Å
Rg (electron density)	39.96 Å
Total Rg	40.57 Å
Atom count	15362
Residues	1910
Excluded volume	276190 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1usy__assembly_1__model_1`	octameric （8）	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 (7)

Entity 1 Entity 1 polymer

Description description	ATP PHOSPHORIBOSYLTRANSFERASE REGULATORY SUBUNIT
Molecular weight formula_weight	31326.6 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,D
Atom count atom_count	15636

MDFLDFEKVFSFYSKATKKGFSPFFVPALEKAEEPAGNFFLDRKGNLFSIREDFTKTVLNHRKRYSPDSQIKVWYADFVYRYSGSDLVAEYQLGLEKVPRNSLDDSLEVLEIIVESASEFFEGPVIVEIGHTGVYEDLLKEIPKDLHEKVLNLIDTKNLAEIEFLSHMKKIDLSRVEKIIEDSIYRRSPEHLKTMDLPLSVREDLLSASSFLQEKFPTVSVEIDLTLARTIEEYCGLIFTIYDTSSSRLVAAGGEYTVNGEKGVGGSIFLEGKTC

Source Source

Source organism organism	THERMOTOGA MARITIMA
NCBI taxonomy ID ncbi_taxonomy_id	243274
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	ATP PHOSPHORIBOSYLTRANSFERASE REGULATORY SUBUNIT
Molecular weight formula_weight	31354.6 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

MDFLDFEKVFSFYSKATKKGFSPFFVPALEKAEEPAGNFFLDRKGNLFSIREDFTKTVLNHRKRYSPESQIKVWYADFVYRYSGSDLVAEYQLGLEKVPRNSLDDSLEVLEIIVESASEFFEGPVIVEIGHTGLYEDLLKEIPKDLHEKVLNLIDTKNLAEIEFLSHMKKIDLSRVEKIIEDSIYRRSPEHLKTMDLPLSVREDLLSASSFLQEKFPTVSVEIDLTLARTIEEYCGLIFTIYDTSSSRLVAAGGEYTVNGEKGVGGSIFLEGKTC

Source Source

Source organism organism	THERMOTOGA MARITIMA
NCBI taxonomy ID ncbi_taxonomy_id	243274
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 polymer

Description description	ATP PHOSPHORIBOSYLTRANSFERASE
Molecular weight formula_weight	23544.4 kDa
EC 编号 ec_number	2.4.2.17
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,G

MLKLAIPKGRLEEKVMTYLKKTGVIFERESSILREGKDIVCFMVRPFDVPTYLVHGVADIGFCGTDVLLEKETSLIQPFFIPTNISRMVLAGPKGRGIPEGEKRIATKFPNVTQRYCESKGWHCRIIPLKGSVELAPIAGLSDLIVDITETGRTLKENNLEILDEIFVIRTHVVVNPVSYRTKREEVVSFLEKLQEVIEHDSNEQSRG

Source Source

Source organism organism	THERMOTOGA MARITIMA
NCBI taxonomy ID ncbi_taxonomy_id	243274
Host organism host_organism	ESCHERICHIA COLI

Entity 4 Entity 4 polymer

Description description	ATP PHOSPHORIBOSYLTRANSFERASE
Molecular weight formula_weight	23544.5 kDa
EC 编号 ec_number	2.4.2.17
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

Source Source

Source organism organism	THERMOTOGA MARITIMA
NCBI taxonomy ID ncbi_taxonomy_id	243274
Host organism host_organism	ESCHERICHIA COLI

Entity 5 Entity 5 non-polymer

Description description	HISTIDINE
Molecular weight formula_weight	156.2 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 6 Entity 6 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	274

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6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d1usya_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.104 — Class II aaRS and biotin synthetases
Superfamily Superfamily superfamily	d.104.1 — Class II aaRS and biotin synthetases
Family Family family	d.104.1.1 — Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain

Domain ID domain_id	d1usyb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.104 — Class II aaRS and biotin synthetases
Superfamily Superfamily superfamily	d.104.1 — Class II aaRS and biotin synthetases
Family Family family	d.104.1.1 — Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain

Domain ID domain_id	d1usyc_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.104 — Class II aaRS and biotin synthetases
Superfamily Superfamily superfamily	d.104.1 — Class II aaRS and biotin synthetases
Family Family family	d.104.1.1 — Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain

Domain ID domain_id	d1usyd_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.104 — Class II aaRS and biotin synthetases
Superfamily Superfamily superfamily	d.104.1 — Class II aaRS and biotin synthetases
Family Family family	d.104.1.1 — Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain

Domain ID domain_id	d1usye_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamily	c.94.1 — Periplasmic binding protein-like II
Family Family family	c.94.1.1 — Phosphate binding protein-like

Domain ID domain_id	d1usyf_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamily	c.94.1 — Periplasmic binding protein-like II
Family Family family	c.94.1.1 — Phosphate binding protein-like

Domain ID domain_id	d1usyg_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamily	c.94.1 — Periplasmic binding protein-like II
Family Family family	c.94.1.1 — Phosphate binding protein-like

Domain ID domain_id	d1usyh_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamily	c.94.1 — Periplasmic binding protein-like II
Family Family family	c.94.1.1 — Phosphate binding protein-like

CATH v4.4 (12 domains)

Domain ID domain_id	1usyA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily	10 — Bira Bifunctional Protein; Domain 2

Domain ID domain_id	1usyB00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily	10 — Bira Bifunctional Protein; Domain 2

Domain ID domain_id	1usyC00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily	10 — Bira Bifunctional Protein; Domain 2

Domain ID domain_id	1usyD00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily	10 — Bira Bifunctional Protein; Domain 2

Domain ID domain_id	1usyE01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	1usyE02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	1usyF01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	1usyF02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	1usyG01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	1usyG02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	1usyH01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	1usyH02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

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Unit-cell length a length_a	101.580 Å
Unit-cell length b length_b	134.403 Å
Unit-cell length c length_c	154.206 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	12

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.520 Å
Low-resolution limit resolution_low	12.000 Å
R factor r_factor	0.2070
R_work r_work	0.2030
R_free r_free	0.2870

ATP phosphoribosyl transferase (HisG:HisZ) complex from Thermotoga maritima

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

ATP PHOSPHORIBOSYLTRANSFERASE REGULATORY SUBUNIT

State in the Current Structure

Other States of the Same Protein in the Database

ATP 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

1usy__assembly_1__model_1

1usy__assembly_1__model_1 | I(q)

1usy__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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (8 domains)

CATH v4.4 (12 domains)

7. Citations (1)

ATP phosphoribosyl transferase (HisG:HisZ) complex from Thermotoga maritima

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

ATP PHOSPHORIBOSYLTRANSFERASE REGULATORY SUBUNIT

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

ATP 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

1usy__assembly_1__model_1

1usy__assembly_1__model_1 | I(q)

1usy__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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (8 domains)

CATH v4.4 (12 domains)

7. Citations (1)