SAXSdb — 2f48

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

diphosphate--fructose-6-phosphate 1-phosphotransferase

Borrelia burgdorferi

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	1,6-di-O-phosphono-beta-D-fructofuranose × 1 ALUMINUM FLUORIDE × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O51052_BORBU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–555； UniProt 1–555 Author chain B； PDBConstruct 1–555； UniProt 1–555

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	2f48
Deposition date deposition_date	2005-11-22
Structure title title	Crystal Structure of A Novel Fructose 1,6-Bisphosphate and AlF3 containing Pyrophosphate-dependent Phosphofructo-1-kinase Complex from Borrelia burgdorferi
Keywords keywords	phosphotransfer, 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.

2f48__assembly_1__model_1

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

Download this curve (.dat)

2f48__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2f48__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	32.39 Å
Rg (electron density)	31.58 Å
Total Rg	32.24 Å
Atom count	8749
Residues	1103
Excluded volume	157450 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2f48__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 (4)

Entity 1 Entity 1 polymer

Description description	diphosphate--fructose-6-phosphate 1-phosphotransferase
Molecular weight formula_weight	62551.8 kDa
EC 编号 ec_number	2.7.1.90
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	9434

MNTSLFKQERQKYIPKLPNILKKDFNNISLVYGENTEAIQDRQALKEFFKNTYGLPIISFTEGESSLSFSKALNIGIILSGGPAPGGHNVISGVFDAIKKFNPNSKLFGFKGGPLGLLENDKIELTESLINSYRNTGGFDIVSSGRTKIETEEHYNKALFVAKENNLNAIIIIGGDDSNTNAAILAEYFKKNGENIQVIGVPKTIDADLRNDHIEISFGFDSATKIYSELIGNLCRDAMSTKKYWHFVKLMGRSASHVALECALKTHPNICIVSEEVLAKKKTLSEIIDEMVSVILKRSLNGDNFGVVIVPEGLIEFIPEVKSLMLELCDIFDKNEGEFKGLNIEKMKEIFVAKLSDYMKGVYLSLPLFIQFELIKSILERDPHGNFNVSRVPTEKLFIEMIQSRLNDMKKRGEYKGSFTPVDHFFGYEGRSAFPSNFDSDYCYSLGYNAVVLILNGLTGYMSCIKNLNLKPTDWIAGGVPLTMLMNMEERYGEKKPVIKKALVDLEGRPFKEFVKNRDKWALNNLYLYPGPVQYFGSSEIVDEITETLKLELFK

Source Source

Source organism organism	Borrelia burgdorferi
NCBI taxonomy ID ncbi_taxonomy_id	224326
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	1,6-di-O-phosphono-beta-D-fructofuranose
Molecular weight formula_weight	340.1 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	ALUMINUM FLUORIDE
Molecular weight formula_weight	84.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	685

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2f48a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.89 — Phosphofructokinase
Superfamily Superfamily superfamily	c.89.1 — Phosphofructokinase
Family Family family	c.89.1.1 — Phosphofructokinase

Domain ID domain_id	d2f48b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.89 — Phosphofructokinase
Superfamily Superfamily superfamily	c.89.1 — Phosphofructokinase
Family Family family	c.89.1.1 — Phosphofructokinase

CATH v4.4 (6 domains)

Domain ID domain_id	2f48A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	450 —

Domain ID domain_id	2f48A02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	460 — Phosphofructokinase domain

Domain ID domain_id	2f48A03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	480 — Phosphofructokinase; domain 3

Domain ID domain_id	2f48B01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	450 —

Domain ID domain_id	2f48B02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	460 — Phosphofructokinase domain

Domain ID domain_id	2f48B03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	480 — Phosphofructokinase; domain 3

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Unit-cell length a length_a	83.411 Å
Unit-cell length b length_b	100.979 Å
Unit-cell length c length_c	150.043 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 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.110 Å
Low-resolution limit resolution_low	58.720 Å
R factor r_factor	0.2030
R_work r_work	0.2000
R_free r_free	0.2579

Crystal Structure of A Novel Fructose 1,6-Bisphosphate and AlF3 containing Pyrophosphate-dependent Phosphofructo-1-kinase Complex from Borrelia burgdorferi

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

diphosphate--fructose-6-phosphate 1-phosphotransferase

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

2f48__assembly_1__model_1

2f48__assembly_1__model_1 | I(q)

2f48__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

CATH v4.4 (6 domains)

7. Citations (1)

Crystal Structure of A Novel Fructose 1,6-Bisphosphate and AlF3 containing Pyrophosphate-dependent Phosphofructo-1-kinase Complex from Borrelia burgdorferi

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

diphosphate--fructose-6-phosphate 1-phosphotransferase

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

2f48__assembly_1__model_1

2f48__assembly_1__model_1 | I(q)

2f48__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

CATH v4.4 (6 domains)

7. Citations (1)