SAXSdb — 1n7v

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

Adsorption protein P2

Enterobacteria phage PRD1

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	ACETATE ION × 4 CALCIUM ION × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	VP02_BPPRD
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； 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	1n7v
Deposition date deposition_date	2002-11-18
Structure title title	THE RECEPTOR-BINDING PROTEIN P2 OF BACTERIOPHAGE PRD1: CRYSTAL FORM III
Keywords keywords	bacteriophage PRD1, viral receptor-binding, beta-propeller, proline-rich, antibiotic-resistance, Viral protein; VIRAL 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.

1n7v__assembly_1__model_1

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

Download this curve (.dat)

1n7v__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1n7v__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	41.24 Å
Rg (electron density)	41.43 Å
Total Rg	41.50 Å
Atom count	7998
Residues	1066
Excluded volume	141430 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1n7v__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	Adsorption protein P2
Molecular weight formula_weight	59925.4 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	4233

ANFNVPKLGVFPVAAVFDIDNVPEDSSATGSRWLPSIYQGGNYWGGGPQALHAQVSNFDSSNRLPYNPRTENNPAGNCAFAFNPFGQYISNISSAQSVHRRIYGIDLNDEPLFSPNAASITNGGNPTMSQDTGYHNIGPINTAYKAEIFRPVNPLPMSDTAPDPETLEPGQTEPLIKSDGVYSNSGIASFIFDRPVTEPNPNWPPLPPPVIPIIYPTPALGIGAAAAYGFGYQVTVYRWEEIPVEFIADPETCPAQPTTDKVIIRTTDLNPEGSPCAYEAGIILVRQTSNPMNAVAGRLVPYVEDIAVDIFLTGKFFTLNPPLRITNNYFADDEVKENTVTIGNYTTTLSSAYYAVYKTDGYGGATCFIASGGAGISALVQLQDNSVLDVLYYSLPLSLGGSKAAIDEWVANNCGLFPMSGGLDKTTLLEIPRRQLEAINPQDGPGQYDLFILDDSGAYASFSSFIGYPEAAYYVAGAATFMDVENPDEIIFILRNGAGWYACEIGDALKIADDEFDSVDYFAYRGGVMFIGSARYTEGGDPLPIKYRAIIPGLP

Source Source

Source organism organism	Enterobacteria phage PRD1
NCBI taxonomy ID ncbi_taxonomy_id	10658
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	ACETATE ION
Molecular weight formula_weight	59.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 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	234

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1n7va_
Class class	b — All beta proteins
Fold Fold fold	b.126 — Adsorption protein p2
Superfamily Superfamily superfamily	b.126.1 — Adsorption protein p2
Family Family family	b.126.1.1 — Adsorption protein p2

CATH v4.4 (3 domains)

Domain ID domain_id	1n7vA01
Class class	2 — Mainly Beta
Architecture architecture	105 — 3 Propeller
Topology topology	10 — Pseudo beta propeller
Homologous superfamily homologous superfamily	10 — Pseudo beta propeller

Domain ID domain_id	1n7vA02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	330 — receptor-binding protein prd1-p2, domain 2
Homologous superfamily homologous superfamily	10 — receptor-binding protein prd1-p2, domain 2

Domain ID domain_id	1n7vA03
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	250 — receptor-binding protein prd1-p2, domain 3
Homologous superfamily homologous superfamily	10 — receptor-binding protein prd1-p2, domain 3

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7. Citations (7)

;The Receptor Binding Protein P2 of PRD1, a Virus Targeting Antibiotic-Resistant Bacteria, Has a Novel Fold Suggesting Multiple Functions. ;

Structure (2003)

PMID: 12623018 · DOI: 10.1016/S0969-2126(03)00023-6 PRIMARY

;A tale of two viruses with therapeutic potential: Structural studies on CELO, an avian adenovirus and the bacteriophage PRD1 ;

Thesis (2002)

;Crystallization and preliminary X-ray analysis of receptor-binding protein P2 of bacteriopahge PRD1 ;

J.STRUCT.BIOL. (2000)

DOI: 10.1006/jsbi.2000.4275

;Stable packing of phage PRD1 DNA requires adsorption protein P2, which binds to the IncP plasmid-encoded conjugative transfer complex ;

J.BACTERIOL. (1999)

Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures

Cell(Cambridge,Mass.) (1999)

DOI: 10.1016/S0092-8674(00)81516-0

Bacteriophage PRD1 contains a labile receptor-binding structure at each vertex

J.Mol.Biol. (1999)

DOI: 10.1006/jmbi.1999.2978

Bacteriophage PRD1: a broad host range dsDNA tectivirus with an internal membrane

Adv.Virus Res. (1995)

Unit-cell length a length_a	46.500 Å
Unit-cell length b length_b	270.200 Å
Unit-cell length c length_c	137.200 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	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	38.110 Å
R factor r_factor	0.2290
R_work r_work	0.2290
R_free r_free	0.2620

THE RECEPTOR-BINDING PROTEIN P2 OF BACTERIOPHAGE PRD1: CRYSTAL FORM III

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

Adsorption protein P2

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

1n7v__assembly_1__model_1

1n7v__assembly_1__model_1 | I(q)

1n7v__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) 4 domains

SCOP 2.08 (1 domains)

CATH v4.4 (3 domains)

7. Citations (7)

THE RECEPTOR-BINDING PROTEIN P2 OF BACTERIOPHAGE PRD1: CRYSTAL FORM III

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

Adsorption protein P2

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

1n7v__assembly_1__model_1

1n7v__assembly_1__model_1 | I(q)

1n7v__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) 4 domains

SCOP 2.08 (1 domains)

CATH v4.4 (3 domains)

7. Citations (7)