SAXSdb — 1sph

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

HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR

Bacillus subtilis

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PTHP_BACSU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–88； UniProt 1–87 Author chain B； PDBConstruct 2–88； UniProt 1–87

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	1sph
Deposition date deposition_date	1994-11-03
Structure title title	REFINED STRUCTURES OF THE ACTIVE S83C AND IMPAIRED S46D HPRS: EVIDENCE THAT PHOSPHORYLATION DOES NOT REQUIRE A BACKBONE CONFORMATIONAL TRANSITION
Keywords keywords	PHOSPHOTRANSFERASE; PHOSPHOTRANSFERASE
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.

1sph__assembly_1__model_1

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

Download this curve (.dat)

1sph__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1sph__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	18.10 Å
Rg (electron density)	17.05 Å
Total Rg	17.84 Å
Atom count	1270
Residues	174
Excluded volume	22513 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1sph__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 (2)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1spha_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.94 — HPr-like
Superfamily Superfamily superfamily	d.94.1 — HPr-like
Family Family family	d.94.1.1 — HPr-like

Domain ID domain_id	d1sphb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.94 — HPr-like
Superfamily Superfamily superfamily	d.94.1 — HPr-like
Family Family family	d.94.1.1 — HPr-like

CATH v4.4 (2 domains)

Domain ID domain_id	1sphA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1340 — Histidine-containing Protein; Chain: A;
Homologous superfamily homologous superfamily	10 — HPr-like

Domain ID domain_id	1sphB00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1340 — Histidine-containing Protein; Chain: A;
Homologous superfamily homologous superfamily	10 — HPr-like

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Unit-cell length a length_a	49.500 Å
Unit-cell length b length_b	25.700 Å
Unit-cell length c length_c	60.400 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	108.90 °
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	2.000 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.1430
R_work r_work	0.1430
R_free r_free	—

Description description	HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR
Molecular weight formula_weight	9226.3 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	1384

REFINED STRUCTURES OF THE ACTIVE S83C AND IMPAIRED S46D HPRS: EVIDENCE THAT PHOSPHORYLATION DOES NOT REQUIRE A BACKBONE CONFORMATIONAL TRANSITION

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

HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR

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

1sph__assembly_1__model_1

1sph__assembly_1__model_1 | I(q)

1sph__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (3)

Source organism organism	Bacillus subtilis
NCBI taxonomy ID ncbi_taxonomy_id	1423

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	114

REFINED STRUCTURES OF THE ACTIVE S83C AND IMPAIRED S46D HPRS: EVIDENCE THAT PHOSPHORYLATION DOES NOT REQUIRE A BACKBONE CONFORMATIONAL TRANSITION

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

HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR

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

1sph__assembly_1__model_1

1sph__assembly_1__model_1 | I(q)

1sph__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (3)