SAXSdb — 1j6t

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

PTS SYSTEM, MANNITOL-SPECIFIC IIABC COMPONENT

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Phosphocarrier protein HPr × 1 （P0AA04） PHOSPHITE ION × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PTM3C_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–148； UniProt 491–637

Phosphocarrier protein HPr

Escherichia coli

UniProt P0AA04

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	PTS SYSTEM, MANNITOL-SPECIFIC IIABC COMPONENT × 1 （P00550） PHOSPHITE ION × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PTHP_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–85； UniProt 1–85

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	1j6t
Deposition date deposition_date	2002-08-14
Structure title title	COMPLEX OF ENZYME IIAMTL AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE
Keywords keywords	PHOSPHOTRANSFERASE, TRANSFERASE, KINASE, SUGAR TRANSPORT, COMPLEX (TRANSFERASE-PHOSPHOCARRIER); TRANSFERASE
Experimental Method method	SOLUTION NMR

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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.

1j6t__assembly_1__model_1

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

Download this curve (.dat)

1j6t__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1j6t__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	19.07 Å
Rg (electron density)	17.98 Å
Total Rg	18.90 Å
Atom count	3534
Residues	229
Excluded volume	31373 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1j6t__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	2	`1j6t__assembly_1__model_2`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	3	`1j6t__assembly_1__model_3`	dimeric （2）	Excluded	—	—
	Exclusion reason： The official assembly declares a ligand or ion, but that component is absent from the generated coordinate model, leaving the structure composition incomplete.

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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	PTS SYSTEM, MANNITOL-SPECIFIC IIABC COMPONENT
Molecular weight formula_weight	16348.5 kDa
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	10673

MANLFKLGAENIFLGRKAATKEEAIRFAGEQLVKGGYVEPEYVQAMLDREKLTPTYLGESIAVPHGTVEAKDRVLKTGVVFCQYPEGVRFGEEEDDIARLVIGIAARNNEHIQVITSLTNALDDESVIERLAHTTSVDEVLELLAGRK

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Phosphocarrier protein HPr
Molecular weight formula_weight	9129.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MFQQEVTITAPNGLHTRPAAQFVKEAKGFTSEITVTSNGKSASAKSLFKLQTLGLTQGTVVTISAEGEDEQKAVEHLVKLMAELE

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	PHOSPHITE ION
Molecular weight formula_weight	79.0 kDa
Source method src_method	syn
Copy count entity_count	1

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1j6ta_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.112 — Phoshotransferase/anion transport protein
Superfamily Superfamily superfamily	d.112.1 — Phoshotransferase/anion transport protein
Family Family family	d.112.1.1 — IIA domain of mannitol-specific and ntr phosphotransferase EII

Domain ID domain_id	d1j6tb_
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	1j6tA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	930 — Mannitol-specific EII; Chain A
Homologous superfamily homologous superfamily	10 — Mannitol-specific EII; Chain A

Domain ID domain_id	1j6tB00
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	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

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

COMPLEX OF ENZYME IIAMTL AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE

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

PTS SYSTEM, MANNITOL-SPECIFIC IIABC COMPONENT

State in the Current Structure

Other States of the Same Protein in the Database

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

1j6t__assembly_1__model_1

1j6t__assembly_1__model_1 | I(q)

1j6t__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

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 non-polymer

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

COMPLEX OF ENZYME IIAMTL AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE

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

PTS SYSTEM, MANNITOL-SPECIFIC IIABC COMPONENT

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

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

1j6t__assembly_1__model_1

1j6t__assembly_1__model_1 | I(q)

1j6t__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

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 non-polymer

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)