2iou

Major Tropism Determinant P1 (Mtd-P1) Variant Complexed with Bordetella brochiseptica Virulence Factor Pertactin extracellular domain (Prn-E).

Method: X-RAY DIFFRACTION

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

Major Tropism Determinant P1

Bordetella phage BPP-1

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 8	Pertactin Extracellular Domain × 2 （Q03035） MAGNESIUM ION × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q775D6_9CAUD
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–376； UniProt 5–380 Author chain B； PDBConstruct 1–376； UniProt 5–380 Author chain C； PDBConstruct 1–376； UniProt 5–380 Author chain D； PDBConstruct 1–376； UniProt 5–380 Author chain E； PDBConstruct 1–376； UniProt 5–380 Author chain F； PDBConstruct 1–376； UniProt 5–380

Pertactin Extracellular Domain

Bordetella bronchiseptica

UniProt Q03035

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 8	Major Tropism Determinant P1 × 6 （Q775D6） MAGNESIUM ION × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PERT_BORBR
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain G； PDBConstruct 1–535； UniProt 38–572 Author chain H； PDBConstruct 1–535； UniProt 38–572

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	2iou
Deposition date deposition_date	2006-10-10
Structure title title	Major Tropism Determinant P1 (Mtd-P1) Variant Complexed with Bordetella brochiseptica Virulence Factor Pertactin extracellular domain (Prn-E).
Keywords keywords	Mtd; Prn; pertactin, viral protein-membrane protein COMPLEX; viral protein/membrane protein
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.

2iou__assembly_1__model_1

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

Download this curve (.dat)

2iou__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2iou__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	61.60 Å
Rg (electron density)	62.24 Å
Total Rg	62.25 Å
Atom count	23900
Residues	3272
Excluded volume	419100 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2iou__assembly_1__model_1`	octameric （8）	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	Major Tropism Determinant P1
Molecular weight formula_weight	39037.9 kDa
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	23900

VQFRGGTTAQHATFTGAAREITVDTDKNTVVVHDGATAGGFPLARHDLVKTAFIKADKSAVAFTRTGNATASIKAGTIVEVNGKLVQFTADTAITMPALTAGTDYAIYVCDDGTVRADSNFSAPTGYTSTTARKVGGFHYAPGSNAAAQAGGNTTAQINEYSLWDIKFRPAALDPRGMTLVAGAFWADIYLLGVNHLTDGTSKYNVTIADGSASPKKSTKFGGDGSAAYSDGAWYNFAEVMTHHGKRLPNYNEFQALAFGTTEATSSGGTDVPTTGVNGTGATSAWNIFTSKWGVVQASGCLWTWGNEFGGVNGASEYTANTGGRGSVYAQPAAALFGGAWNGTSLSGSRAALWYSGPSFSFAFFGARGVCDHLIL

Source Source

Source organism organism	Bordetella phage BPP-1
NCBI taxonomy ID ncbi_taxonomy_id	194699
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Pertactin Extracellular Domain
Molecular weight formula_weight	54486.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

DWNNQSIIKAGERQHGIHIKQSDGAGVRTATGTTIKVSGRQAQGVLLENPAAELRFQNGSVTSSGQLFDEGVRRFLGTVTVKAGKLVADHATLANVSDTRDDDGIALYVAGEQAQASIADSTLQGAGGVRVERGANVTVQRSTIVDGGLHIGTLQPLQPEDLPPSRVVLGDTSVTAVPASGAPAAVSVFGANELTVDGGHITGGRAAGVAAMDGAIVHLQRATIRRGDAPAGGAVPGGAVPGGAVPGGFGPLLDGWYGVDVSDSTVDLAQSIVEAPQLGAAIRAGRGARVTVSGGSLSAPHGNVIETGGGARRFPPPASPLSITLQAGARAQGRALLYRVLPEPVKLTLAGGAQGQGDIVATELPPIPGASSGPLDVALASQARWTGATRAVDSLSIDNATWVMTDNSNVGALRLASDGSVDFQQPAEAGRFKVLMVDTLAGSGLFRMNVFADLGLSDKLVVMRDASGQHRLWVRNSGSEPASANTMLLVQTPRGSAATFTLANKDGKVDIGTYRYRLAANGNGQWSLVGAKAPP

Source Source

Source organism organism	Bordetella bronchiseptica
NCBI taxonomy ID ncbi_taxonomy_id	257310
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	4

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6. Fold Classification (SCOP + CATH) 34 domains

SCOP 2.08 (14 domains)

Domain ID domain_id	d2ioua1
Class class	b — All beta proteins
Fold Fold fold	b.163 — Pseudo beta-prism I
Superfamily Superfamily superfamily	b.163.1 — Bacteriophage trimeric proteins domain
Family Family family	b.163.1.1 — Mtd domain-like

Domain ID domain_id	d2ioua2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.169 — C-type lectin-like
Superfamily Superfamily superfamily	d.169.1 — C-type lectin-like
Family Family family	d.169.1.8 — Mtd variable domain

Domain ID domain_id	d2ioub1
Class class	b — All beta proteins
Fold Fold fold	b.163 — Pseudo beta-prism I
Superfamily Superfamily superfamily	b.163.1 — Bacteriophage trimeric proteins domain
Family Family family	b.163.1.1 — Mtd domain-like

Domain ID domain_id	d2ioub2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.169 — C-type lectin-like
Superfamily Superfamily superfamily	d.169.1 — C-type lectin-like
Family Family family	d.169.1.8 — Mtd variable domain

Domain ID domain_id	d2iouc1
Class class	b — All beta proteins
Fold Fold fold	b.163 — Pseudo beta-prism I
Superfamily Superfamily superfamily	b.163.1 — Bacteriophage trimeric proteins domain
Family Family family	b.163.1.1 — Mtd domain-like

Domain ID domain_id	d2iouc2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.169 — C-type lectin-like
Superfamily Superfamily superfamily	d.169.1 — C-type lectin-like
Family Family family	d.169.1.8 — Mtd variable domain

Domain ID domain_id	d2ioud1
Class class	b — All beta proteins
Fold Fold fold	b.163 — Pseudo beta-prism I
Superfamily Superfamily superfamily	b.163.1 — Bacteriophage trimeric proteins domain
Family Family family	b.163.1.1 — Mtd domain-like

Domain ID domain_id	d2ioud2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.169 — C-type lectin-like
Superfamily Superfamily superfamily	d.169.1 — C-type lectin-like
Family Family family	d.169.1.8 — Mtd variable domain

Domain ID domain_id	d2ioue1
Class class	b — All beta proteins
Fold Fold fold	b.163 — Pseudo beta-prism I
Superfamily Superfamily superfamily	b.163.1 — Bacteriophage trimeric proteins domain
Family Family family	b.163.1.1 — Mtd domain-like

Domain ID domain_id	d2ioue2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.169 — C-type lectin-like
Superfamily Superfamily superfamily	d.169.1 — C-type lectin-like
Family Family family	d.169.1.8 — Mtd variable domain

Domain ID domain_id	d2iouf1
Class class	b — All beta proteins
Fold Fold fold	b.163 — Pseudo beta-prism I
Superfamily Superfamily superfamily	b.163.1 — Bacteriophage trimeric proteins domain
Family Family family	b.163.1.1 — Mtd domain-like

Domain ID domain_id	d2iouf2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.169 — C-type lectin-like
Superfamily Superfamily superfamily	d.169.1 — C-type lectin-like
Family Family family	d.169.1.8 — Mtd variable domain

Domain ID domain_id	d2ioug_
Class class	b — All beta proteins
Fold Fold fold	b.80 — Single-stranded right-handed beta-helix
Superfamily Superfamily superfamily	b.80.1 — Pectin lyase-like
Family Family family	b.80.1.7 — Virulence factor P.69 pertactin

Domain ID domain_id	d2iouh_
Class class	b — All beta proteins
Fold Fold fold	b.80 — Single-stranded right-handed beta-helix
Superfamily Superfamily superfamily	b.80.1 — Pectin lyase-like
Family Family family	b.80.1.7 — Virulence factor P.69 pertactin

CATH v4.4 (20 domains)

Domain ID domain_id	2iouA01
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	10 — Seminal Fluid Protein PDC-109 (Domain B)
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	2iouA02
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	20 — Tail fiber receptor-binding protein
Homologous superfamily homologous superfamily	10 — Tail fiber receptor-binding protein

Domain ID domain_id	2iouA03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1580 — paralog of FGE (formylglycine-generating enzyme)
Homologous superfamily homologous superfamily	10 — paralog of FGE (formylglycine-generating enzyme)

Domain ID domain_id	2iouB01
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	10 — Seminal Fluid Protein PDC-109 (Domain B)
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	2iouB02
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	20 — Tail fiber receptor-binding protein
Homologous superfamily homologous superfamily	10 — Tail fiber receptor-binding protein

Domain ID domain_id	2iouB03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1580 — paralog of FGE (formylglycine-generating enzyme)
Homologous superfamily homologous superfamily	10 — paralog of FGE (formylglycine-generating enzyme)

Domain ID domain_id	2iouC01
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	10 — Seminal Fluid Protein PDC-109 (Domain B)
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	2iouC02
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	20 — Tail fiber receptor-binding protein
Homologous superfamily homologous superfamily	10 — Tail fiber receptor-binding protein

Domain ID domain_id	2iouC03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1580 — paralog of FGE (formylglycine-generating enzyme)
Homologous superfamily homologous superfamily	10 — paralog of FGE (formylglycine-generating enzyme)

Domain ID domain_id	2iouD01
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	10 — Seminal Fluid Protein PDC-109 (Domain B)
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	2iouD02
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	20 — Tail fiber receptor-binding protein
Homologous superfamily homologous superfamily	10 — Tail fiber receptor-binding protein

Domain ID domain_id	2iouD03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1580 — paralog of FGE (formylglycine-generating enzyme)
Homologous superfamily homologous superfamily	10 — paralog of FGE (formylglycine-generating enzyme)

Domain ID domain_id	2iouE01
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	10 — Seminal Fluid Protein PDC-109 (Domain B)
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	2iouE02
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	20 — Tail fiber receptor-binding protein
Homologous superfamily homologous superfamily	10 — Tail fiber receptor-binding protein

Domain ID domain_id	2iouE03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1580 — paralog of FGE (formylglycine-generating enzyme)
Homologous superfamily homologous superfamily	10 — paralog of FGE (formylglycine-generating enzyme)

Domain ID domain_id	2iouF01
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	10 — Seminal Fluid Protein PDC-109 (Domain B)
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	2iouF02
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	20 — Tail fiber receptor-binding protein
Homologous superfamily homologous superfamily	10 — Tail fiber receptor-binding protein

Domain ID domain_id	2iouF03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1580 — paralog of FGE (formylglycine-generating enzyme)
Homologous superfamily homologous superfamily	10 — paralog of FGE (formylglycine-generating enzyme)

Domain ID domain_id	2iouG00
Class class	2 — Mainly Beta
Architecture architecture	160 — 3 Solenoid
Topology topology	20 — Pectate Lyase C-like
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	2iouH00
Class class	2 — Mainly Beta
Architecture architecture	160 — 3 Solenoid
Topology topology	20 — Pectate Lyase C-like
Homologous superfamily homologous superfamily	20 —

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Unit-cell length a length_a	413.464 Å
Unit-cell length b length_b	413.464 Å
Unit-cell length c length_c	98.859 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	36

Space group space_group	P 61
Space-group number int_tables_number	169
Crystal system crystal_system	—

Resolution resolution	3.160 Å
Low-resolution limit resolution_low	49.630 Å
R factor r_factor	0.2253
R_work r_work	0.2240
R_free r_free	0.2493

Major Tropism Determinant P1 (Mtd-P1) Variant Complexed with Bordetella brochiseptica Virulence Factor Pertactin extracellular domain (Prn-E).

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

Major Tropism Determinant P1

State in the Current Structure

Other States of the Same Protein in the Database

Pertactin Extracellular Domain

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

2iou__assembly_1__model_1

2iou__assembly_1__model_1 | I(q)

2iou__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 (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) 34 domains

SCOP 2.08 (14 domains)

CATH v4.4 (20 domains)

7. Citations (1)

Major Tropism Determinant P1 (Mtd-P1) Variant Complexed with Bordetella brochiseptica Virulence Factor Pertactin extracellular domain (Prn-E).

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

Major Tropism Determinant P1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Pertactin Extracellular Domain

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

2iou__assembly_1__model_1

2iou__assembly_1__model_1 | I(q)

2iou__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 (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) 34 domains

SCOP 2.08 (14 domains)

CATH v4.4 (20 domains)

7. Citations (1)