2bsq

FitAB bound to DNA

Method: X-RAY DIFFRACTION

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

TRAFFICKING PROTEIN B

NEISSERIA GONORRHOEAE

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 8 DNA 2	TRAFFICKING PROTEIN A × 4 （Q5F881） IR36, FORWARD STRAND × 1 IR36, REVERSE STRAND × 1 water × 9	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q5F882_NEIG1
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–139； UniProt 1–139 Author chain B； PDBConstruct 1–139； UniProt 1–139 Author chain C； PDBConstruct 1–139； UniProt 1–139 Author chain D； PDBConstruct 1–139； UniProt 1–139

TRAFFICKING PROTEIN A

NEISSERIA GONORRHOEAE

UniProt Q5F881

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 8 DNA 2	TRAFFICKING PROTEIN B × 4 （Q5F882） IR36, FORWARD STRAND × 1 IR36, REVERSE STRAND × 1 water × 9	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q5F881_NEIG1
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–77； UniProt 2–78 Author chain F； PDBConstruct 1–77； UniProt 2–78 Author chain G； PDBConstruct 1–77； UniProt 2–78 Author chain H； PDBConstruct 1–77； UniProt 2–78

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	2bsq
Deposition date deposition_date	2005-05-23
Structure title title	FitAB bound to DNA
Keywords keywords	TRANSCRIPTION, TRANSCRIPTION REGULATION COMPLEX, PIN DOMAIN, RIBBON-HELIX-HELIX, DNA BINDING, HETERODIMER; TRANSCRIPTION
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.

2bsq__assembly_1__model_1

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

Download this curve (.dat)

2bsq__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2bsq__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	36.78 Å
Rg (electron density)	35.71 Å
Total Rg	36.22 Å
Atom count	7865
Residues	906
Excluded volume	136020 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2bsq__assembly_1__model_1`	decameric （10）	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 (5)

Entity 1 Entity 1 polymer

Description description	TRAFFICKING PROTEIN B
Molecular weight formula_weight	16333.8 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	7910

MILLDTNVISEPLRPQPNERVVAWLDSLILEDVYLSAITVAEMRLGVALLLNGKKKNVLHERMEQSILPLFAGRILPFDEPVAAIYAQIRSYAKTHGKEIAAADGYIAATAKQHSMTVATRDTGSFFAADVAVFNPWHLEHHHHHH

Source Source

Source organism organism	NEISSERIA GONORRHOEAE
NCBI taxonomy ID ncbi_taxonomy_id	485
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	TRAFFICKING PROTEIN A
Molecular weight formula_weight	8313.4 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

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

ASVVIRNLSEATHNAIKFRARAAGRSTEAEIRLILDNIAKAQQTVRLGSMLASIGQEIGGVELEDVRGRNTDNEVSL

Source Source

Source organism organism	NEISSERIA GONORRHOEAE
NCBI taxonomy ID ncbi_taxonomy_id	485
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 polymer

Description description	IR36, FORWARD STRAND
Molecular weight formula_weight	11170.0 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	I

AGATTGCTATCATTTTTTTTATTTTGATAGCATUTG

Entity 4 Entity 4 polymer

Description description	IR36, REVERSE STRAND
Molecular weight formula_weight	11198.1 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	J

CAAATGCTATCAAAAUAAAAAAAATGATAGCAATCT

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	45

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6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (12 domains)

Domain ID domain_id	d2bsqa1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.120 — PIN domain-like
Superfamily Superfamily superfamily	c.120.1 — PIN domain-like
Family Family family	c.120.1.1 — PIN domain

Domain ID domain_id	d2bsqa2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2bsqb1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.120 — PIN domain-like
Superfamily Superfamily superfamily	c.120.1 — PIN domain-like
Family Family family	c.120.1.1 — PIN domain

Domain ID domain_id	d2bsqb2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2bsqc1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.120 — PIN domain-like
Superfamily Superfamily superfamily	c.120.1 — PIN domain-like
Family Family family	c.120.1.1 — PIN domain

Domain ID domain_id	d2bsqc2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2bsqd1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.120 — PIN domain-like
Superfamily Superfamily superfamily	c.120.1 — PIN domain-like
Family Family family	c.120.1.1 — PIN domain

Domain ID domain_id	d2bsqd2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2bsqe1
Class class	a — All alpha proteins
Fold Fold fold	a.43 — Ribbon-helix-helix
Superfamily Superfamily superfamily	a.43.1 — Ribbon-helix-helix
Family Family family	a.43.1.8 — Trafficking protein A-like

Domain ID domain_id	d2bsqf1
Class class	a — All alpha proteins
Fold Fold fold	a.43 — Ribbon-helix-helix
Superfamily Superfamily superfamily	a.43.1 — Ribbon-helix-helix
Family Family family	a.43.1.8 — Trafficking protein A-like

Domain ID domain_id	d2bsqg1
Class class	a — All alpha proteins
Fold Fold fold	a.43 — Ribbon-helix-helix
Superfamily Superfamily superfamily	a.43.1 — Ribbon-helix-helix
Family Family family	a.43.1.8 — Trafficking protein A-like

Domain ID domain_id	d2bsqh1
Class class	a — All alpha proteins
Fold Fold fold	a.43 — Ribbon-helix-helix
Superfamily Superfamily superfamily	a.43.1 — Ribbon-helix-helix
Family Family family	a.43.1.8 — Trafficking protein A-like

CATH v4.4 (8 domains)

Domain ID domain_id	2bsqA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1010 — 5'-nuclease

Domain ID domain_id	2bsqB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1010 — 5'-nuclease

Domain ID domain_id	2bsqC00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1010 — 5'-nuclease

Domain ID domain_id	2bsqD00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1010 — 5'-nuclease

Domain ID domain_id	2bsqE01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1220 — Arc Repressor Mutant
Homologous superfamily homologous superfamily	10 — Met repressor-like

Domain ID domain_id	2bsqF01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1220 — Arc Repressor Mutant
Homologous superfamily homologous superfamily	10 — Met repressor-like

Domain ID domain_id	2bsqG01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1220 — Arc Repressor Mutant
Homologous superfamily homologous superfamily	10 — Met repressor-like

Domain ID domain_id	2bsqH01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1220 — Arc Repressor Mutant
Homologous superfamily homologous superfamily	10 — Met repressor-like

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Unit-cell length a length_a	75.040 Å
Unit-cell length b length_b	82.403 Å
Unit-cell length c length_c	135.503 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	94.19 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	70.360 Å
R factor r_factor	0.2130
R_work r_work	0.2130
R_free r_free	0.2710

FitAB bound to DNA

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

TRAFFICKING PROTEIN B

State in the Current Structure

Other States of the Same Protein in the Database

TRAFFICKING PROTEIN A

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

2bsq__assembly_1__model_1

2bsq__assembly_1__model_1 | I(q)

2bsq__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 (5)

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

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (12 domains)

CATH v4.4 (8 domains)

7. Citations (1)

FitAB bound to DNA

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

TRAFFICKING PROTEIN B

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

TRAFFICKING PROTEIN A

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

2bsq__assembly_1__model_1

2bsq__assembly_1__model_1 | I(q)

2bsq__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 (5)

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

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (12 domains)

CATH v4.4 (8 domains)

7. Citations (1)