SAXSdb — 1wmi

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

hypothetical protein PHS013

Pyrococcus horikoshii

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	hypothetical protein PHS014 × 2 （O73967） water × 4	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 8	hypothetical protein PHS014 × 4 （O73967） water × 8	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 4	hypothetical protein PHS014 × 2 （O73967） water × 4	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 4	hypothetical protein PHS014 × 2 （O73967） water × 4	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 2	hypothetical protein PHS014 × 1 （O73967） water × 2	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 2	hypothetical protein PHS014 × 1 （O73967） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O73966_PYRHO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–90； UniProt 1–90 Author chain C； PDBConstruct 1–90； UniProt 1–90

hypothetical protein PHS014

Pyrococcus horikoshii

UniProt O73967

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	hypothetical protein PHS013 × 2 （O73966） water × 4	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 8	hypothetical protein PHS013 × 4 （O73966） water × 8	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 4	hypothetical protein PHS013 × 2 （O73966） water × 4	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 4	hypothetical protein PHS013 × 2 （O73966） water × 4	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 2	hypothetical protein PHS013 × 1 （O73966） water × 2	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 2	hypothetical protein PHS013 × 1 （O73966） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O73967_PYRHO
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–67； UniProt 1–67 Author chain D； PDBConstruct 1–67； UniProt 1–67

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	1wmi
Deposition date deposition_date	2004-07-09
Structure title title	Crystal structure of archaeal RelE-RelB complex from Pyrococcus horikoshii OT3
Keywords keywords	toxin-antitoxin complex, HYDROLASE-HYDROLASE INHIBITOR COMPLEX; HYDROLASE/HYDROLASE INHIBITOR
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.

1wmi__assembly_3__model_1

Assembly 3 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1wmi__assembly_3__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1wmi__assembly_3__model_1 | P(r) · Pending

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

Rg（Guinier）	21.32 Å
Rg (electron density)	20.00 Å
Total Rg	21.00 Å
Atom count	2508
Residues	298
Excluded volume	44904 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1wmi__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1wmi__assembly_2__model_1`	octameric （8）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1wmi__assembly_3__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1wmi__assembly_4__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`1wmi__assembly_5__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`1wmi__assembly_6__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	hypothetical protein PHS013
Molecular weight formula_weight	10904.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	2544

MTYRVKIHKQVVKALQSLPKAHYRRFLEFRDILEYEPVPREKFDVIKLEGTGDLDLYRARLGDYRVIYSVNWKDKVIKILKLKPRGRAYK

Source Source

Source organism organism	Pyrococcus horikoshii
NCBI taxonomy ID ncbi_taxonomy_id	70601
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	hypothetical protein PHS014
Molecular weight formula_weight	8002.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

MRMEKVGDVLKELERLKVEIQRLEAMLMPEERDEDITEEEIAELLELARDEDPENWIDAEELPEPED

Source Source

Source organism organism	Pyrococcus horikoshii
NCBI taxonomy ID ncbi_taxonomy_id	70601
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	36

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1wmia1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.298 — RelE-like
Superfamily Superfamily superfamily	d.298.1 — RelE-like
Family Family family	d.298.1.2 — RelE-like

Domain ID domain_id	d1wmib1
Class class	a — All alpha proteins
Fold Fold fold	a.137 — Non-globular all-alpha subunits of globular proteins
Superfamily Superfamily superfamily	a.137.13 — RelB-like
Family Family family	a.137.13.1 — RelB-like

Domain ID domain_id	d1wmic_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.298 — RelE-like
Superfamily Superfamily superfamily	d.298.1 — RelE-like
Family Family family	d.298.1.2 — RelE-like

Domain ID domain_id	d1wmid_
Class class	a — All alpha proteins
Fold Fold fold	a.137 — Non-globular all-alpha subunits of globular proteins
Superfamily Superfamily superfamily	a.137.13 — RelB-like
Family Family family	a.137.13.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id	1wmiA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2310 — YaeB-like fold
Homologous superfamily homologous superfamily	20 — RelE-like

Domain ID domain_id	1wmiB00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	250 —

Domain ID domain_id	1wmiC00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2310 — YaeB-like fold
Homologous superfamily homologous superfamily	20 — RelE-like

Domain ID domain_id	1wmiD00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	250 —

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Unit-cell length a length_a	47.533 Å
Unit-cell length b length_b	142.651 Å
Unit-cell length c length_c	37.168 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	8

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	—
R_work r_work	0.2280
R_free r_free	0.2760

Crystal structure of archaeal RelE-RelB complex from Pyrococcus horikoshii OT3

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

hypothetical protein PHS013

State in the Current Structure

Other States of the Same Protein in the Database

hypothetical protein PHS014

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

1wmi__assembly_3__model_1

1wmi__assembly_3__model_1 | I(q)

1wmi__assembly_3__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 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Crystal structure of archaeal RelE-RelB complex from Pyrococcus horikoshii OT3

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

hypothetical protein PHS013

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

hypothetical protein PHS014

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

1wmi__assembly_3__model_1

1wmi__assembly_3__model_1 | I(q)

1wmi__assembly_3__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 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)