SAXSdb — 8u11

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

Packaged DNA stabilization protein gp10

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 58	Tail spike protein × 18 （P12528） Portal protein × 12 （P26744） Peptidoglycan hydrolase gp4 × 12 （P26746） Major capsid protein × 10 （P26747）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	VG10_BPP22
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 1； PDBConstruct 1–472； UniProt 1–472 Author chain 2； PDBConstruct 1–472； UniProt 1–472 Author chain 3； PDBConstruct 1–472； UniProt 1–472 Author chain 4； PDBConstruct 1–472； UniProt 1–472 Author chain 5； PDBConstruct 1–472； UniProt 1–472 Author chain 6； PDBConstruct 1–472； UniProt 1–472

Tail spike protein

OrganismNot specified

UniProt P12528

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 58	Packaged DNA stabilization protein gp10 × 6 （P26749） Portal protein × 12 （P26744） Peptidoglycan hydrolase gp4 × 12 （P26746） Major capsid protein × 10 （P26747）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FIBER_BPP22
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain 10； PDBConstruct 1–667； UniProt 1–667 Author chain 11； PDBConstruct 1–667； UniProt 1–667 Author chain 12； PDBConstruct 1–667； UniProt 1–667 Author chain 13； PDBConstruct 1–667； UniProt 1–667 Author chain 14； PDBConstruct 1–667； UniProt 1–667 Author chain 15； PDBConstruct 1–667； UniProt 1–667 Author chain 16； PDBConstruct 1–667； UniProt 1–667 Author chain 17； PDBConstruct 1–667； UniProt 1–667 Author chain 18； PDBConstruct 1–667； UniProt 1–667 Author chain 19； PDBConstruct 1–667； UniProt 1–667 Author chain 20； PDBConstruct 1–667； UniProt 1–667 Author chain 21； PDBConstruct 1–667； UniProt 1–667 Author chain 22； PDBConstruct 1–667； UniProt 1–667 Author chain 23； PDBConstruct 1–667； UniProt 1–667 Author chain 24； PDBConstruct 1–667； UniProt 1–667 Author chain 7； PDBConstruct 1–667； UniProt 1–667 Author chain 8； PDBConstruct 1–667； UniProt 1–667 Author chain 9； PDBConstruct 1–667； UniProt 1–667

Portal protein

OrganismNot specified

UniProt P26744

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 58	Packaged DNA stabilization protein gp10 × 6 （P26749） Tail spike protein × 18 （P12528） Peptidoglycan hydrolase gp4 × 12 （P26746） Major capsid protein × 10 （P26747）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PORTL_BPP22
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain a； PDBConstruct 1–725； UniProt 1–725 Author chain b； PDBConstruct 1–725； UniProt 1–725 Author chain c； PDBConstruct 1–725； UniProt 1–725 Author chain d； PDBConstruct 1–725； UniProt 1–725 Author chain e； PDBConstruct 1–725； UniProt 1–725 Author chain f； PDBConstruct 1–725； UniProt 1–725 Author chain g； PDBConstruct 1–725； UniProt 1–725 Author chain h； PDBConstruct 1–725； UniProt 1–725 Author chain i； PDBConstruct 1–725； UniProt 1–725 Author chain j； PDBConstruct 1–725； UniProt 1–725 Author chain k； PDBConstruct 1–725； UniProt 1–725 Author chain l； PDBConstruct 1–725； UniProt 1–725

Peptidoglycan hydrolase gp4

OrganismNot specified

UniProt P26746

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 58	Packaged DNA stabilization protein gp10 × 6 （P26749） Tail spike protein × 18 （P12528） Portal protein × 12 （P26744） Major capsid protein × 10 （P26747）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	EXLYS_BPP22
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain m； PDBConstruct 1–166； UniProt 1–166 Author chain n； PDBConstruct 1–166； UniProt 1–166 Author chain o； PDBConstruct 1–166； UniProt 1–166 Author chain p； PDBConstruct 1–166； UniProt 1–166 Author chain q； PDBConstruct 1–166； UniProt 1–166 Author chain r； PDBConstruct 1–166； UniProt 1–166 Author chain s； PDBConstruct 1–166； UniProt 1–166 Author chain t； PDBConstruct 1–166； UniProt 1–166 Author chain u； PDBConstruct 1–166； UniProt 1–166 Author chain v； PDBConstruct 1–166； UniProt 1–166 Author chain x； PDBConstruct 1–166； UniProt 1–166 Author chain y； PDBConstruct 1–166； UniProt 1–166

Major capsid protein

OrganismNot specified

UniProt P26747

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 58	Packaged DNA stabilization protein gp10 × 6 （P26749） Tail spike protein × 18 （P12528） Portal protein × 12 （P26744） Peptidoglycan hydrolase gp4 × 12 （P26746）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CAPSD_BPP22
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain A； PDBConstruct 1–430； UniProt 1–430 Author chain B； PDBConstruct 1–430； UniProt 1–430 Author chain C； PDBConstruct 1–430； UniProt 1–430 Author chain D； PDBConstruct 1–430； UniProt 1–430 Author chain E； PDBConstruct 1–430； UniProt 1–430 Author chain F； PDBConstruct 1–430； UniProt 1–430 Author chain G； PDBConstruct 1–430； UniProt 1–430 Author chain H； PDBConstruct 1–430； UniProt 1–430 Author chain I； PDBConstruct 1–430； UniProt 1–430 Author chain J； PDBConstruct 1–430； UniProt 1–430

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	8u11
Deposition date deposition_date	2023-08-30
Structure title title	In situ cryo-EM structure of bacteriophage P22 gp1:gp5:gp4: gp10: gp9 N-term complex in conformation 2 at 3.1A resolution
Keywords keywords	;phage, bacteriophage, tail spike protein, TSP, gene product 9 (gp9), Packaged DNA stabilization protein, gene product 10 (gp10), STRUCTURAL PROTEIN, VIRAL PROTEIN, head-to-tail protein, gene product 4 (gp4), Tail hub protein, gene product (1), Portal protein, Coat protein, Major capsid protein, gene product 5 (gp5) ;; VIRAL PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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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.

8u11__assembly_1__model_1

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

Download this curve (.dat)

8u11__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

8u11__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	86.11 Å
Rg (electron density)	85.41 Å
Total Rg	85.48 Å
Atom count	138386
Residues	17588
Excluded volume	2450600 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`8u11__assembly_1__model_1`	58-meric （58）	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	Packaged DNA stabilization protein gp10
Molecular weight formula_weight	52512.0 kDa
Source method src_method	nat
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1,2,3,4,5,6
Atom count atom_count	138386

MPIQQLPMMKGMGKDFKNADYIDYLPVNMLATPKEILNSSGYLRSFPGITKRYDMNGVSRGVEYNTAQNAVYRVCGGKLYKGESEVGDVAGSGRVSMAHGRTSQAVGVNGQLVEYRYDGTVKTVSNWPADSGFTQYELGSVRDITRLRGRYAWSKDGTDSWFITDLEDESHPDRYSAQYRAESQPDGIIGIGTWRDFIVCFGSSTIEYFSLTGATTAGAALYVAQPSLMVQKGIAGTYCKTPFADSYAFISHPATGAPSVYIIGSGQASPIATASIEKIIRSYTAEEMATGVMETLRFDSHELLIIHLPRHVLVYDASSSQNGPQWCVLKTGLYDDVYRGVDFMYEGNQITCGDKSEAVVGQLQFDISSQYDKQQEHLLFTPLFKADNARCFDLEVESSTGVAQYADRLFLSATTDGINYGREQMIEQNEPFVYDKRVLWKRVGRIRRLIGFKLRVITKSPVTLSGCQIRLE

Entity 2 Entity 2 polymer

Description description	Tail spike protein
Molecular weight formula_weight	71923.5 kDa
Source method src_method	nat
Copy count entity_count	18

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	7,8,9,10,11,12,13,14,15,16,17,18,19,20,21,22,23,24

MTDITANVVVSNPRPIFTESRSFKAVANGKIYIGQIDTDPVNPANQIPVYIENEDGSHVQITQPLIINAAGKIVYNGQLVKIVTVQGHSMAIYDANGSQVDYIANVLKYDPDQYSIEADKKFKYSVKLSDYPTLQDAASAAVDGLLIDRDYNFYGGETVDFGGKVLTIECKAKFIGDGNLIFTKLGKGSRIAGVFMESTTTPWVIKPWTDDNQWLTDAAAVVATLKQSKTDGYQPTVSDYVKFPGIETLLPPNAKGQNITSTLEIRECIGVEVHRASGLMAGFLFRGCHFCKMVDANNPSGGKDGIITFENLSGDWGKGNYVIGGRTSYGSVSSAQFLRNNGGFERDGGVIGFTSYRAGESGVKTWQGTVGSTTSRNYNLQFRDSVVIYPVWDGFDLGADTDMNPELDRPGDYPITQYPLHQLPLNHLIDNLLVRGALGVGFGMDGKGMYVSNITVEDCAGSGAYLLTHESVFTNIAIIDTNTKDFQANQIYISGACRVNGLRLIGIRSTDGQGLTIDAPNSTVSGITGMVDPSRINVANLAEEGLGNIRANSFGYDSAAIKLRIHKLSKTLDSGALYSHINGGAGSGSAYTQLTAISGSTPDAVSLKVNHKDCRGAEIPFVPDIASDDFIKDSSCFLPYWENNSTSLKALVKKPNGELVRLTLATL

Entity 3 Entity 3 polymer

Description description	Portal protein
Molecular weight formula_weight	82829.4 kDa
Source method src_method	nat
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	a,b,c,d,e,l,f,k,i,j,h,g

MADNENRLESILSRFDADWTASDEARREAKNDLFFSRVSQWDDWLSQYTTLQYRGQFDVVRPVVRKLVSEMRQNPIDVLYRPKDGARPDAADVLMGMYRTDMRHNTAKIAVNIAVREQIEAGVGAWRLVTDYEDQSPTSNNQVIRREPIHSACSHVIWDSNSKLMDKSDARHCTVIHSMSQNGWEDFAEKYDLDADDIPSFQNPNDWVFPWLTQDTIQIAEFYEVVEKKETAFIYQDPVTGEPVSYFKRDIKDVIDDLADSGFIKIAERQIKRRRVYKSIITCTAVLKDKQLIAGEHIPIVPVFGEWGFVEDKEVYEGVVRLTKDGQRLRNMIMSFNADIVARTPKKKPFFWPEQIAGFEHMYDGNDDYPYYLLNRTDENSGDLPTQPLAYYENPEVPQANAYMLEAATSAVKEVATLGVDTEAVNGGQVAFDTVNQLNMRADLETYVFQDNLATAMRRDGEIYQSIVNDIYDVPRNVTITLEDGSEKDVQLMAEVVDLATGEKQVLNDIRGRYECYTDVGPSFQSMKQQNRAEILELLGKTPQGTPEYQLLLLQYFTLLDGKGVEMMRDYANKQLIQMGVKKPETPEEQQWLVEAQQAKQGQQDPAMVQAQGVLLQGQAELAKAQNQTLSLQIDAAKVEAQNQLNAARIAEIFNNMDLSKQSEFREFLKTVASFQQDRSEDARANAELLLKGDEQTHKQRMDIANILQSQRQNQPSGSVAETPQ

Entity 4 Entity 4 polymer

Description description	Peptidoglycan hydrolase gp4
Molecular weight formula_weight	18045.0 kDa
Source method src_method	nat
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	y,m,n,o,p,q,r,s,t,u,v,x

MQIKTKGDLVRAALRKLGVASDATLTDVEPQSMQDAVDDLEAMMAEWYQDGKGIITGYVFSDDENPPAEGDDHGLRSSAVSAVFHNLACRIAPDYALEATAKIIATAKYGKELLYKQTAISRAKRAPYPSRMPTGSGNSFANLNEWHYFPGEQNADSTTPHDEGNG

Entity 5 Entity 5 polymer

Description description	Major capsid protein
Molecular weight formula_weight	46795.6 kDa
Source method src_method	nat
Copy count entity_count	10

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,C,A,G,I,D,B,F,H,J

MALNEGQIVTLAVDEIIETISAITPMAQKAKKYTPPAASMQRSSNTIWMPVEQESPTQEGWDLTDKATGLLELNVAVNMGEPDNDFFQLRADDLRDETAYRRRIQSAARKLANNVELKVANMAAEMGSLVITSPDAIGTNTADAWNFVADAEEIMFSRELNRDMGTSYFFNPQDYKKAGYDLTKRDIFGRIPEEAYRDGTIQRQVAGFDDVLRSPKLPVLTKSTATGITVSGAQSFKPVAWQLDNDGNKVNVDNRFATVTLSATTGMKRGDKISFAGVKFLGQMAKNVLAQDATFSVVRVVDGTHVEITPKPVALDDVSLSPEQRAYANVNTSLADAMAVNILNVKDARTNVFWADDAIRIVSQPIPANHELFAGMKTTSFSIPDVGLNGIFATQGDISTLSGLCRIALWYGVNATRPEAIGVGLPGQTA

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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	—

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

Resolution resolution	3.10 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	17944

In situ cryo-EM structure of bacteriophage P22 gp1:gp5:gp4: gp10: gp9 N-term complex in conformation 2 at 3.1A resolution

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

Packaged DNA stabilization protein gp10

State in the Current Structure

Other States of the Same Protein in the Database

Tail spike protein

State in the Current Structure

Other States of the Same Protein in the Database

Portal protein

State in the Current Structure

Other States of the Same Protein in the Database

Peptidoglycan hydrolase gp4

State in the Current Structure

Other States of the Same Protein in the Database

Major capsid protein

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

8u11__assembly_1__model_1

8u11__assembly_1__model_1 | I(q)

8u11__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

7. Citations (1)

In situ cryo-EM structure of bacteriophage P22 gp1:gp5:gp4: gp10: gp9 N-term complex in conformation 2 at 3.1A resolution

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

Packaged DNA stabilization protein gp10

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Tail spike protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Portal protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Peptidoglycan hydrolase gp4

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Major capsid protein

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

8u11__assembly_1__model_1

8u11__assembly_1__model_1 | I(q)

8u11__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

7. Citations (1)