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8u11

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

Method: ELECTRON MICROSCOPY Dmax: 295.2 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Packaged DNA stabilization protein gp10

OrganismNot specified

UniProt P26749

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 58 PDB declaration: 58-meric（58） Consistent with protein copy count Chain 1； UniProt 1–472 Chain 2； UniProt 1–472 Chain 3； UniProt 1–472 Chain 4； UniProt 1–472 Chain 5； UniProt 1–472 Chain 6； UniProt 1–472 Not recorded Tail spike protein × 18 （P12528） Portal protein × 12 （P26744） Peptidoglycan hydrolase gp4 × 12 （P26746） Major capsid protein × 10 （P26747） ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 8U11 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8EAP Cryo-EM structure of the in-situ gp10-gp26 from bacteriophage P22 Deposited 2022-08-29 Different construct Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric
Chain D 2–472（471 aa）
Chain E 2–472（471 aa）
Chain F 2–472（471 aa）
Chain G 2–472（471 aa）
Chain H 2–472（471 aa）
Chain I 2–472（471 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
8EB7 Cryo-EM structure of the in-situ gp4-gp10-gp9N from bacteriophage P22 Deposited 2022-08-30 Different construct Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric
Chain R 2–472（471 aa）
Chain S 2–472（471 aa）
Chain T 2–472（471 aa）
Chain U 2–472（471 aa）
Chain V 2–472（471 aa）
Chain W 2–472（471 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
8TVR In situ cryo-EM structure of bacteriophage P22 tail hub protein: tailspike protein complex at 2.8A resolution Deposited 2023-08-18 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric
Chain G 1–472（472 aa）
Chain K 1–472（472 aa）
Chain O 1–472（472 aa）
Chain S 1–472（472 aa）
Chain T 1–472（472 aa）
Chain Y 1–472（472 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
8U10 In situ cryo-EM structure of bacteriophage P22 gp1:gp4:gp5:gp10:gp9 N-term complex in conformation 1 at 3.2A resolution Deposited 2023-08-30 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric
Chain 1 1–472（472 aa）
Chain 2 1–472（472 aa）
Chain 3 1–472（472 aa）
Chain 4 1–472（472 aa）
Chain 5 1–472（472 aa）
Chain 6 1–472（472 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 58 PDB declaration: 58-meric（58） Consistent with protein copy count Chain 10； UniProt 1–667 Chain 11； UniProt 1–667 Chain 12； UniProt 1–667 Chain 13； UniProt 1–667 Chain 14； UniProt 1–667 Chain 15； UniProt 1–667 Chain 16； UniProt 1–667 Chain 17； UniProt 1–667 Chain 18； UniProt 1–667 Chain 19； UniProt 1–667 Chain 20； UniProt 1–667 Chain 21； UniProt 1–667 Chain 22； UniProt 1–667 Chain 23； UniProt 1–667 Chain 24； UniProt 1–667 Chain 7； UniProt 1–667 Chain 8； UniProt 1–667 Chain 9； UniProt 1–667 Not recorded Packaged DNA stabilization protein gp10 × 6 （P26749） Portal protein × 12 （P26744） Peptidoglycan hydrolase gp4 × 12 （P26746） Major capsid protein × 10 （P26747） ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 8U11 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CLW TAILSPIKE PROTEIN FROM PHAGE P22, V331A MUTANT Deposited 1999-05-04 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–667（554 aa） Fragment：CATALYTIC FRAGMENT
Mutation：V331A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 10；pH 10.00
Resolution 2.00 Å
1CLW TAILSPIKE PROTEIN FROM PHAGE P22, V331A MUTANT Deposited 1999-05-04 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 114–667（554 aa） Fragment：CATALYTIC FRAGMENT
Mutation：V331A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 10；pH 10.00
Resolution 2.00 Å
1LKT CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEIN Deposited 1997-10-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 6–109（104 aa） Fragment：HEAD-BINDING DOMAIN
Chain B 6–109（104 aa） Fragment：HEAD-BINDING DOMAIN
Chain C 6–109（104 aa） Fragment：HEAD-BINDING DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.6；20% PEG 8K, 0.2 M MGCL2, 0.1 M BIS-TRIS, PH 6.6
Resolution 2.60 Å
1LKT CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEIN Deposited 1997-10-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain D 6–109（104 aa） Fragment：HEAD-BINDING DOMAIN
Chain E 6–109（104 aa） Fragment：HEAD-BINDING DOMAIN
Chain F 6–109（104 aa） Fragment：HEAD-BINDING DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.6；20% PEG 8K, 0.2 M MGCL2, 0.1 M BIS-TRIS, PH 6.6
Resolution 2.60 Å
1QA1 TAILSPIKE PROTEIN, MUTANT V331G Deposited 1999-04-10 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–667（554 aa） Fragment：RECEPTOR BINDING C-TERMINAL DOMAIN
Mutation：V331G No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；274 K；VAPOR DIFFUSION, HANGING DROP, 274 K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE
Resolution 2.00 Å
1QA1 TAILSPIKE PROTEIN, MUTANT V331G Deposited 1999-04-10 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 114–667（554 aa） Fragment：RECEPTOR BINDING C-TERMINAL DOMAIN
Mutation：V331G No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；274 K；VAPOR DIFFUSION, HANGING DROP, 274 K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE
Resolution 2.00 Å
1QA2 TAILSPIKE PROTEIN, MUTANT A334V Deposited 1999-04-10 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–667（554 aa） Fragment：RECEPTOR BINDING C-TERMINAL FRAGMENT
Mutation：A334V No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；VAPOR DIFFUSION, HANGING DROP, 277K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE
Resolution 2.00 Å
1QA2 TAILSPIKE PROTEIN, MUTANT A334V Deposited 1999-04-10 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 114–667（554 aa） Fragment：RECEPTOR BINDING C-TERMINAL FRAGMENT
Mutation：A334V No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；VAPOR DIFFUSION, HANGING DROP, 277K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE
Resolution 2.00 Å
1QA3 TAILSPIKE PROTEIN, MUTANT A334I Deposited 1999-04-10 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–667（554 aa） Fragment：RECEPTOR BINDING C-TERMINAL FRAGMENT
Mutation：A334I No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；VAPOR DIFFUSION, HANGING DROP, 277K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE
Resolution 2.00 Å
1QA3 TAILSPIKE PROTEIN, MUTANT A334I Deposited 1999-04-10 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 114–667（554 aa） Fragment：RECEPTOR BINDING C-TERMINAL FRAGMENT
Mutation：A334I No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；VAPOR DIFFUSION, HANGING DROP, 277K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE
Resolution 2.00 Å
1QQ1 TAILSPIKE PROTEIN, MUTANT E359G Deposited 1999-06-10 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 109–667（559 aa） Fragment：C-TERMINAL FRAGMENT
Mutation：E359G No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；293 K；1M AMMONIUM SULPHATE, 0.1M SODIUM PHOSPHATE, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.80 Å
1QRB PLASTICITY AND STERIC STRAIN IN A PARALLEL BETA-HELIX: RATIONAL MUTATIONS IN P22 TAILSPIKE PROTEIN Deposited 1999-06-12 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 109–667（559 aa） Fragment：C-TERMINAL FRAGMENT
Mutation：T326F No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；293 K；1M AMMONIUM SULPHATE 0.1 M SODIUM PHOSPHATE, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.00 Å
1QRC TAILSPIKE PROTEIN, MUTANT W391A Deposited 1999-06-13 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 109–667（559 aa） Fragment：C-TERMINAL FRAGMENT
Mutation：W391A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；293 K；1M AMMONIUM SULPHATE, 0.1M NA-PHOSPHATE, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.50 Å
1TSP CRYSTAL STRUCTURE OF P22 TAILSPIKE PROTEIN: INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER Deposited 1994-06-16 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 109–667（559 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1TYU STRUCTURE OF TAILSPIKE-PROTEIN Deposited 1996-07-26 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 114–667（554 aa） Fragment：RESIDUES 109-666 LACKING THE N-TERMINAL, HEAD-BINDING DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；COMPLEX FORMED BY SOAKING WITH 2MM OCTASACCHARIDE FROM SALMONELLA ENTERITIDIS AT PH 7.5
Resolution 1.80 Å
1TYV STRUCTURE OF TAILSPIKE-PROTEIN Deposited 1996-07-26 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 114–667（554 aa） Fragment：RESIDUES 109-666 LACKING THE N-TERMINAL, HEAD-BINDING DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 1.80 Å
1TYW STRUCTURE OF TAILSPIKE-PROTEIN Deposited 1996-07-26 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 114–667（554 aa） Fragment：RESIDUES 109-666 LACKING THE N-TERMINAL, HEAD-BINDING DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；COMPLEX FORMED BY SOAKING WITH DECASACCHARIDE FROM S. TYPHI 253TY O-ANTIGEN AT PH 7.5
Resolution 1.80 Å
1TYX TITLE OF TAILSPIKE-PROTEIN Deposited 1996-07-26 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 114–667（554 aa） Fragment：RESIDUES 109-666 LACKING THE N-TERMINAL, HEAD-BINDING DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；COMPLEX FORMED BY SOAKING WITH 2MM OCTASACCHARIDE FROM SALMONELLA TYPHIMURIUM O-ANTIGEN AT PH 7.5.
Resolution 1.80 Å
2VFM Low Temperature Structure of P22 Tailspike Protein Fragment (109-666) Deposited 2007-11-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 110–667（558 aa） Fragment：RESIDUES 110-667
Not recorded GOL GLYCEROL × 33 SO4 SULFATE ION × 6 CA CALCIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 10；DROP: 2 MICROLITER 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0, PLUS 3.3 MICROLITER 10 MG/ML PROTEIN SOLUTION IN 10 MM HEPES, PH 7.0; RESERVOIR: 750 MICOLITER 1.0 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0
Resolution 1.50 Å R-free 0.164
2VFN Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125A Deposited 2007-11-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 110–667（558 aa） Fragment：RESIDUES 110-667
Mutation：YES GOL GLYCEROL × 30 SO4 SULFATE ION × 3 CA CALCIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 10；DROP: 2 MICROLITER 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0, PLUS 3.3 MICROLITER, 10 MG/ML PROTEIN SOLUTION IN 10 MM HEPES, PH 7.0; RESERVOIR: 750 MICOLITER 1.0 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0
Resolution 1.50 Å R-free 0.155
2VFO Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125L Deposited 2007-11-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 110–667（558 aa） Fragment：RESIDUES 110-667
Mutation：YES GOL GLYCEROL × 21 SO4 SULFATE ION × 3 CA CALCIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 10；DROP: 2 MICROLITER 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0, PLUS 3.3 MICROLITER 10 MG/ML PROTEIN SOLUTION IN 10 MM HEPES, PH 7.0; RESERVOIR: 750 MICOLITER 1.0 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0
Resolution 1.50 Å R-free 0.144
2VFP Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V349L Deposited 2007-11-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 110–667（558 aa） Fragment：RESIDUES 110-667
Mutation：YES GOL GLYCEROL × 18 SO4 SULFATE ION × 3 CA CALCIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 10；DROP: 2 MICROLITER 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0, PLUS 3.3 MICROLITER 10 MG/ML PROTEIN SOLUTION IN 10 MM HEPES, PH 7.0; RESERVOIR: 750 MICOLITER 1.0 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0
Resolution 1.55 Å R-free 0.152
2VFQ Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V450A Deposited 2007-11-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 110–667（558 aa） Fragment：RESIDUES 110-667 LACKING THE N-TERMINAL HEAD-BINDING DOMAIN
Mutation：YES GOL GLYCEROL × 12 SO4 SULFATE ION × 6 CA CALCIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 10；DROP: 2 MICROLITER 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0, PLUS 3.3 MICROLITER 10 MG/ML PROTEIN SOLUTION IN 10 MM HEPES, PH 7.0; RESERVOIR: 750 MICOLITER 1.0 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0
Resolution 1.55 Å R-free 0.145
2VKY Headbinding Domain of Phage P22 Tailspike C-Terminally Fused to Isoleucine Zipper pIIGCN4 (Chimera I) Deposited 2008-01-04 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain B 2–124（123 aa） Fragment：HEAD-BINDING DOMAIN, RESIDUES 2-124
Mutation：YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；VAPOR DIFFUSION, HANGING DROP. PROTEIN: CONC. 8.2 MG/ML,BUFFER 50MM HEPES, PH6.5; RESERVOIR: 20% ISOPROPANOL, 0.1M NA-ACETATE, PH4.6, 0.2M CACL2; DROPLET 2 MICROL: 2 MICROL.CRYO:30% GLYCEROL.
Resolution 2.05 Å R-free 0.187
2VNL MUTANT Y108Wdel OF THE HEADBINDING DOMAIN OF PHAGE P22 TAILSPIKE C- TERMINally fused to ISOLEUCINE ZIPPER pIIGCN4 (chimera II) Deposited 2008-02-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 2–122（121 aa） Fragment：HEAD-BINDING DOMAIN, RESIDUES 2-122
Mutation：YES GOL GLYCEROL × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；VAPOR DIFFUSION, HANGING DROP. PROTEIN: CONC. 9.3 MG/ML,BUFFER 50MM HEPES, PH6.5; RESERVOIR:20% ISOPROPANOL, 0.1M NA-ACETATE, PH4.6, 0.2M CACL2; DROPLET 2 MICROL:2 MICROL.CRYO:30% GLYCEROL.
Resolution 1.80 Å R-free 0.229
2XC1 Full-length Tailspike Protein Mutant Y108W of Bacteriophage P22 Deposited 2010-04-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 2–667（666 aa） Fragment：RESIDUES 2-667
Chain B 2–667（666 aa） Fragment：RESIDUES 2-667
Chain C 2–667（666 aa） Fragment：RESIDUES 2-667
Mutation：YES Mutation：YES Mutation：YES GOL GLYCEROL × 13 CA CALCIUM ION × 1 PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 4 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；292 K；PROTEIN- 15MG/ML IN 10MM HEPES PH7;RESERVOIR:750 ML 0.2M AMMONIUM ACETATE,0.1M TRI-SODIUM CITRATE DIHYDRATE PH 5.6, 30% W/V POLYETHYLENE GLYCOL 4000; HANGING DROPS:1.5MICROL RESERVOIR- 1.5MICROL PROTEIN SOLUTION; TEMPERATURE: 19 DEGR.; CRYO: 3% GLYCEROL
Resolution 1.65 Å R-free 0.210
3TH0 P22 Tailspike complexed with S.Paratyphi O antigen octasaccharide Deposited 2011-08-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 109–667（559 aa） Fragment：UNP residues 109-657
Not recorded GOL GLYCEROL × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277.15 K；1.5 Ammonium sulfate, 0.1M sodium phosphate over reservoir 1.0 Ammonium sulfate, 0.1M sodium phosphate, pH 10, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K
X-ray crystallization conditions MICRODIALYSIS；pH 7.5；293.15 K；addition of 2mM S.Paratyphi o antigen octasaccharide in 0.1M Tris, 1M sodium phosphate, pH 7.5, MICRODIALYSIS, temperature 293.15K
Resolution 1.75 Å R-free 0.156
5GAI Probabilistic Structural Models of Mature P22 Bacteriophage Portal, Hub, and Tailspike proteins Deposited 2015-12-01 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain 0 6–667（662 aa）
Chain Y 6–667（662 aa）
Chain Z 6–667（662 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE；Blot for 2 seconds before plunging.
Resolution 10.50 Å
8EAN Cryo-EM structure of in-situ tailspike in bacteriophage P22 Deposited 2022-08-29 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain 0 6–667（662 aa）
Chain Y 6–667（662 aa）
Chain Z 6–667（662 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.70 Å
8EB7 Cryo-EM structure of the in-situ gp4-gp10-gp9N from bacteriophage P22 Deposited 2022-08-30 Different construct Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric
Chain 0 6–116（111 aa）
Chain A 6–116（111 aa）
Chain B 6–116（111 aa）
Chain C 6–116（111 aa）
Chain D 6–116（111 aa）
Chain F 6–116（111 aa）
Chain X 6–116（111 aa）
Chain Y 6–116（111 aa）
Chain Z 6–116（111 aa）
Chain a 6–116（111 aa）
Chain b 6–116（111 aa）
Chain c 6–116（111 aa）
Chain d 6–116（111 aa）
Chain e 6–116（111 aa）
Chain f 6–116（111 aa）
Chain g 6–116（111 aa）
Chain h 6–116（111 aa）
Chain i 6–116（111 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
8TVR In situ cryo-EM structure of bacteriophage P22 tail hub protein: tailspike protein complex at 2.8A resolution Deposited 2023-08-18 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric
Chain A 1–667（667 aa）
Chain B 1–667（667 aa）
Chain C 1–667（667 aa）
Chain D 1–667（667 aa）
Chain E 1–667（667 aa）
Chain F 1–667（667 aa）
Chain H 1–667（667 aa）
Chain I 1–667（667 aa）
Chain J 1–667（667 aa）
Chain L 1–667（667 aa）
Chain M 1–667（667 aa）
Chain N 1–667（667 aa）
Chain P 1–667（667 aa）
Chain Q 1–667（667 aa）
Chain R 1–667（667 aa）
Chain V 1–667（667 aa）
Chain W 1–667（667 aa）
Chain X 1–667（667 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
8U10 In situ cryo-EM structure of bacteriophage P22 gp1:gp4:gp5:gp10:gp9 N-term complex in conformation 1 at 3.2A resolution Deposited 2023-08-30 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric
Chain 10 1–667（667 aa）
Chain 11 1–667（667 aa）
Chain 12 1–667（667 aa）
Chain 13 1–667（667 aa）
Chain 14 1–667（667 aa）
Chain 15 1–667（667 aa）
Chain 16 1–667（667 aa）
Chain 17 1–667（667 aa）
Chain 18 1–667（667 aa）
Chain 19 1–667（667 aa）
Chain 20 1–667（667 aa）
Chain 21 1–667（667 aa）
Chain 22 1–667（667 aa）
Chain 23 1–667（667 aa）
Chain 24 1–667（667 aa）
Chain 7 1–667（667 aa）
Chain 8 1–667（667 aa）
Chain 9 1–667（667 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
8U1O In situ cryo-EM structure of bacteriophage P22 tailspike protein complex at 3.4A resolution Deposited 2023-09-01 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain o 1–667（667 aa）
Chain p 1–667（667 aa）
Chain q 1–667（667 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å

28 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 58 PDB declaration: 58-meric（58） Consistent with protein copy count Chain a； UniProt 1–725 Chain b； UniProt 1–725 Chain c； UniProt 1–725 Chain d； UniProt 1–725 Chain e； UniProt 1–725 Chain f； UniProt 1–725 Chain g； UniProt 1–725 Chain h； UniProt 1–725 Chain i； UniProt 1–725 Chain j； UniProt 1–725 Chain k； UniProt 1–725 Chain l； UniProt 1–725 Not recorded Packaged DNA stabilization protein gp10 × 6 （P26749） Tail spike protein × 18 （P12528） Peptidoglycan hydrolase gp4 × 12 （P26746） Major capsid protein × 10 （P26747） ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 8U11 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3LJ5 Full Length Bacteriophage P22 Portal Protein Deposited 2010-01-25 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 1–725（725 aa） Fragment：UNP residues 1-725
Chain B 1–725（725 aa） Fragment：UNP residues 1-725
Chain C 1–725（725 aa） Fragment：UNP residues 1-725
Chain D 1–725（725 aa） Fragment：UNP residues 1-725
Chain E 1–725（725 aa） Fragment：UNP residues 1-725
Chain F 1–725（725 aa） Fragment：UNP residues 1-725
Chain G 1–725（725 aa） Fragment：UNP residues 1-725
Chain H 1–725（725 aa） Fragment：UNP residues 1-725
Chain I 1–725（725 aa） Fragment：UNP residues 1-725
Chain J 1–725（725 aa） Fragment：UNP residues 1-725
Chain K 1–725（725 aa） Fragment：UNP residues 1-725
Chain L 1–725（725 aa） Fragment：UNP residues 1-725
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；293 K；30% tert-Butanol, 70mM sodium chloride, 2.5% PEG 400, 0.1M sodium acetate, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 7.50 Å R-free 0.263
4V4K Bacteriophage P22 Portal Protein bound to middle Tail Factor GP4. This file contain the second biological assembly Deposited 2010-04-19 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric
Chain M 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain N 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain O 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain P 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain Q 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain R 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain S 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain T 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain U 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain V 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain W 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain X 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；20% PEG 8000, 0.1M (NH4)2HPO4, 0.1M MES, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
Resolution 3.25 Å R-free 0.236
4V4K Bacteriophage P22 Portal Protein bound to middle Tail Factor GP4. This file contain the second biological assembly Deposited 2010-04-19 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric
Chain A 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain B 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain C 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain D 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain E 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain F 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain G 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain H 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain I 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain J 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain K 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Chain L 1–602（602 aa） Fragment：UNP RESIDUES 1-602
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；20% PEG 8000, 0.1M (NH4)2HPO4, 0.1M MES, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
Resolution 3.25 Å R-free 0.236
5GAI Probabilistic Structural Models of Mature P22 Bacteriophage Portal, Hub, and Tailspike proteins Deposited 2015-12-01 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain A 5–725（721 aa）
Chain B 5–725（721 aa）
Chain C 5–725（721 aa）
Chain D 5–725（721 aa）
Chain E 5–725（721 aa）
Chain F 5–725（721 aa）
Chain G 5–725（721 aa）
Chain H 5–725（721 aa）
Chain I 5–725（721 aa）
Chain J 5–725（721 aa）
Chain W 5–725（721 aa）
Chain X 5–725（721 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE；Blot for 2 seconds before plunging.
Resolution 10.50 Å
5JJ1 Structure of the Immature Procapsid Conformation of P22 Portal Protein Deposited 2016-04-22 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 1–602（602 aa） Fragment：UNP residues 1-602
Chain B 1–602（602 aa） Fragment：UNP residues 1-602
Chain C 1–602（602 aa） Fragment：UNP residues 1-602
Chain D 1–602（602 aa） Fragment：UNP residues 1-602
Chain E 1–602（602 aa） Fragment：UNP residues 1-602
Chain F 1–602（602 aa） Fragment：UNP residues 1-602
Chain G 1–602（602 aa） Fragment：UNP residues 1-602
Chain H 1–602（602 aa） Fragment：UNP residues 1-602
Chain I 1–602（602 aa） Fragment：UNP residues 1-602
Chain J 1–602（602 aa） Fragment：UNP residues 1-602
Chain K 1–602（602 aa） Fragment：UNP residues 1-602
Chain L 1–602（602 aa） Fragment：UNP residues 1-602
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；5% PEG 8,000, 10 mM Cesium Chloride
Resolution 3.30 Å R-free 0.315
5JJ3 Refined Structure of the Mature Virion Conformation of P22 Portal Protein Deposited 2016-04-22 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 1–725（725 aa）
Chain B 1–725（725 aa）
Chain C 1–725（725 aa）
Chain D 1–725（725 aa）
Chain E 1–725（725 aa）
Chain F 1–725（725 aa）
Chain G 1–725（725 aa）
Chain H 1–725（725 aa）
Chain I 1–725（725 aa）
Chain J 1–725（725 aa）
Chain K 1–725（725 aa）
Chain L 1–725（725 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；30% tert-butanol, 70 mM sodium chloride, 2.5% PEG400 in 0.1 M sodium acetate
Resolution 7.00 Å R-free 0.260
8EAO Cryo-EM structure of the in-situ gp1-gp4 complex from bacteriophage P22 Deposited 2022-08-29 Different construct Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric
Chain B 6–626（621 aa）
Chain D 6–626（621 aa）
Chain F 6–626（621 aa）
Chain H 6–626（621 aa）
Chain J 6–626（621 aa）
Chain L 6–626（621 aa）
Chain N 6–626（621 aa）
Chain P 6–626（621 aa）
Chain R 6–626（621 aa）
Chain T 6–626（621 aa）
Chain V 6–626（621 aa）
Chain X 6–626（621 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
8TVU In situ cryo-EM structure of bacteriophage P22 portal protein: head-to-tail protein complex at 3.0A resolution Deposited 2023-08-18 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric
Chain A 1–725（725 aa）
Chain B 1–725（725 aa）
Chain D 1–725（725 aa）
Chain F 1–725（725 aa）
Chain H 1–725（725 aa）
Chain J 1–725（725 aa）
Chain L 1–725（725 aa）
Chain N 1–725（725 aa）
Chain P 1–725（725 aa）
Chain R 1–725（725 aa）
Chain T 1–725（725 aa）
Chain W 1–725（725 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
8U10 In situ cryo-EM structure of bacteriophage P22 gp1:gp4:gp5:gp10:gp9 N-term complex in conformation 1 at 3.2A resolution Deposited 2023-08-30 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric
Chain a 1–725（725 aa）
Chain b 1–725（725 aa）
Chain c 1–725（725 aa）
Chain d 1–725（725 aa）
Chain e 1–725（725 aa）
Chain f 1–725（725 aa）
Chain g 1–725（725 aa）
Chain h 1–725（725 aa）
Chain i 1–725（725 aa）
Chain j 1–725（725 aa）
Chain k 1–725（725 aa）
Chain l 1–725（725 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
9KYW The scaffold C-loop of phage P22 Deposited 2024-12-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 1–725（725 aa）
Chain L 1–725（725 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.70 Å
9PDP In situ cryoEM structure of bacteriophage P22 portal barrel Deposited 2025-06-30 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: 12-meric
Chain A 602–710（109 aa）
Chain B 602–710（109 aa）
Chain C 602–710（109 aa）
Chain D 602–710（109 aa）
Chain E 602–710（109 aa）
Chain F 602–710（109 aa）
Chain G 602–710（109 aa）
Chain H 602–710（109 aa）
Chain I 602–710（109 aa）
Chain J 602–710（109 aa）
Chain K 602–710（109 aa）
Chain L 602–710（109 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.83 Å
9PGG Cryo-EM structure of bacteriophage P22 gp1-gp5-gp4 complex at 2.76 angstrom Deposited 2025-07-07 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 39 PDB declaration: 39-meric
Chain Bb 1–725（725 aa）
Chain Bd 1–725（725 aa）
Chain Bf 1–725（725 aa）
Chain Bh 1–725（725 aa）
Chain Bj 1–725（725 aa）
Chain Bl 1–725（725 aa）
Chain Bn 1–725（725 aa）
Chain Bp 1–725（725 aa）
Chain Br 1–725（725 aa）
Chain Bt 1–725（725 aa）
Chain Bv 1–725（725 aa）
Chain Bx 1–725（725 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.76 Å

11 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 58 PDB declaration: 58-meric（58） Consistent with protein copy count Chain m； UniProt 1–166 Chain n； UniProt 1–166 Chain o； UniProt 1–166 Chain p； UniProt 1–166 Chain q； UniProt 1–166 Chain r； UniProt 1–166 Chain s； UniProt 1–166 Chain t； UniProt 1–166 Chain u； UniProt 1–166 Chain v； UniProt 1–166 Chain x； UniProt 1–166 Chain y； UniProt 1–166 Not recorded Packaged DNA stabilization protein gp10 × 6 （P26749） Tail spike protein × 18 （P12528） Portal protein × 12 （P26744） Major capsid protein × 10 （P26747） ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 8U11 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4V4K Bacteriophage P22 Portal Protein bound to middle Tail Factor GP4. This file contain the second biological assembly Deposited 2010-04-19 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric
Chain k 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain l 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain m 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain n 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain o 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain p 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain q 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain r 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain s 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain t 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain u 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain v 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；20% PEG 8000, 0.1M (NH4)2HPO4, 0.1M MES, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
Resolution 3.25 Å R-free 0.236
4V4K Bacteriophage P22 Portal Protein bound to middle Tail Factor GP4. This file contain the second biological assembly Deposited 2010-04-19 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric
Chain Y 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain Z 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain a 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain b 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain c 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain d 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain e 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain f 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain g 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain h 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain i 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Chain j 1–166（166 aa） Fragment：UNP RESIDUES 1-166
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；20% PEG 8000, 0.1M (NH4)2HPO4, 0.1M MES, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
Resolution 3.25 Å R-free 0.236
5GAI Probabilistic Structural Models of Mature P22 Bacteriophage Portal, Hub, and Tailspike proteins Deposited 2015-12-01 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain K 5–150（146 aa）
Chain L 5–150（146 aa）
Chain M 5–150（146 aa）
Chain N 5–150（146 aa）
Chain O 5–150（146 aa）
Chain P 5–150（146 aa）
Chain Q 5–150（146 aa）
Chain R 5–150（146 aa）
Chain S 5–150（146 aa）
Chain T 5–150（146 aa）
Chain U 5–150（146 aa）
Chain V 5–150（146 aa）
Mutation：P150A Mutation：P150A Mutation：P150A Mutation：P150A Mutation：P150A Mutation：P150A Mutation：P150A Mutation：P150A Mutation：P150A Mutation：P150A Mutation：P150A Mutation：P150A No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE；Blot for 2 seconds before plunging.
Resolution 10.50 Å
8EAO Cryo-EM structure of the in-situ gp1-gp4 complex from bacteriophage P22 Deposited 2022-08-29 Different construct Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric
Chain A 3–151（149 aa）
Chain C 3–151（149 aa）
Chain E 3–151（149 aa）
Chain G 3–151（149 aa）
Chain I 3–151（149 aa）
Chain K 3–151（149 aa）
Chain M 3–151（149 aa）
Chain O 3–151（149 aa）
Chain Q 3–151（149 aa）
Chain S 3–151（149 aa）
Chain U 3–151（149 aa）
Chain W 3–151（149 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
8EB7 Cryo-EM structure of the in-situ gp4-gp10-gp9N from bacteriophage P22 Deposited 2022-08-30 Different construct Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric
Chain E 2–151（150 aa）
Chain G 2–151（150 aa）
Chain H 2–151（150 aa）
Chain I 2–151（150 aa）
Chain J 2–151（150 aa）
Chain K 2–151（150 aa）
Chain L 2–151（150 aa）
Chain M 2–151（150 aa）
Chain N 2–151（150 aa）
Chain O 2–151（150 aa）
Chain P 2–151（150 aa）
Chain Q 2–151（150 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
8TVU In situ cryo-EM structure of bacteriophage P22 portal protein: head-to-tail protein complex at 3.0A resolution Deposited 2023-08-18 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric
Chain C 1–166（166 aa）
Chain E 1–166（166 aa）
Chain G 1–166（166 aa）
Chain I 1–166（166 aa）
Chain K 1–166（166 aa）
Chain M 1–166（166 aa）
Chain O 1–166（166 aa）
Chain Q 1–166（166 aa）
Chain S 1–166（166 aa）
Chain V 1–166（166 aa）
Chain X 1–166（166 aa）
Chain a 1–166（166 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
8U10 In situ cryo-EM structure of bacteriophage P22 gp1:gp4:gp5:gp10:gp9 N-term complex in conformation 1 at 3.2A resolution Deposited 2023-08-30 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric
Chain m 1–166（166 aa）
Chain n 1–166（166 aa）
Chain o 1–166（166 aa）
Chain p 1–166（166 aa）
Chain q 1–166（166 aa）
Chain r 1–166（166 aa）
Chain s 1–166（166 aa）
Chain t 1–166（166 aa）
Chain u 1–166（166 aa）
Chain v 1–166（166 aa）
Chain x 1–166（166 aa）
Chain y 1–166（166 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
9PGG Cryo-EM structure of bacteriophage P22 gp1-gp5-gp4 complex at 2.76 angstrom Deposited 2025-07-07 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 39 PDB declaration: 39-meric
Chain Ap 1–166（166 aa）
Chain Aq 1–166（166 aa）
Chain Ar 1–166（166 aa）
Chain As 1–166（166 aa）
Chain At 1–166（166 aa）
Chain Au 1–166（166 aa）
Chain Av 1–166（166 aa）
Chain Aw 1–166（166 aa）
Chain Ax 1–166（166 aa）
Chain Ay 1–166（166 aa）
Chain Az 1–166（166 aa）
Chain Ba 1–166（166 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.76 Å

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 58 PDB declaration: 58-meric（58） Consistent with protein copy count Chain A； UniProt 1–430 Chain B； UniProt 1–430 Chain C； UniProt 1–430 Chain D； UniProt 1–430 Chain E； UniProt 1–430 Chain F； UniProt 1–430 Chain G； UniProt 1–430 Chain H； UniProt 1–430 Chain I； UniProt 1–430 Chain J； UniProt 1–430 Not recorded Packaged DNA stabilization protein gp10 × 6 （P26749） Tail spike protein × 18 （P12528） Portal protein × 12 （P26744） Peptidoglycan hydrolase gp4 × 12 （P26746） ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 8U11 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2M5S High-resolution NMR structure and cryo-EM imaging support multiple functional roles for the accessory I-domain of phage P22 coat protein Deposited 2013-03-05 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 223–345（123 aa） Fragment：;This domain has previously been called the 'extra-density domain' and 'telokin-like domain' in the literature based on cryo-EM models ;
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；310.15 K；Ionic strength (raw mmCIF value) 20；Pressure ambient
NMR sample composition 1.5 mM [U-100% 13C; U-100% 15N] protein, 20 mM sodium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.5 mM [U-100% 13C; U-100% 15N] protein, 20 mM sodium phosphate, 1% H2O/99% D2O | 1% H2O/99% D2O
Resolution not provided
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 360 PDB declaration: 360-MERIC
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6
cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE
Resolution 8.20 Å
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6
cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE
Resolution 8.20 Å
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 30 PDB declaration: 30-meric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6
cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE
Resolution 8.20 Å
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 36 PDB declaration: 36-meric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6
cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE
Resolution 8.20 Å
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6
cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE
Resolution 8.20 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 420 PDB declaration: 420-meric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Chain G 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6
cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE
Resolution 9.10 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Chain G 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6
cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE
Resolution 9.10 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 35 PDB declaration: 35-meric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Chain G 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6
cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE
Resolution 9.10 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 42 PDB declaration: 42-meric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Chain G 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6
cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE
Resolution 9.10 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Chain G 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6
cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE
Resolution 9.10 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 420 PDB declaration: 420-meric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Chain G 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl
cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration
Resolution 3.30 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Chain G 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl
cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration
Resolution 3.30 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 35 PDB declaration: 35-meric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Chain G 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl
cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration
Resolution 3.30 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 42 PDB declaration: 42-meric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Chain G 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl
cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration
Resolution 3.30 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Chain G 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl
cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration
Resolution 3.30 Å
8GN5 Designed pH-responsive P22 VLP Deposited 2022-08-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 4–428（425 aa）
Chain B 4–428（425 aa）
Chain C 4–428（425 aa）
Chain D 4–428（425 aa）
Mutation：S43H, E54H, E153H, N287H Mutation：S43H, E54H, E153H, N287H Mutation：S43H, E54H, E153H, N287H Mutation：S43H, E54H, E153H, N287H No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.02 Å
8I1T The asymmetric unit of P22 empty capsid Deposited 2023-01-13 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Chain G 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
8I1V The asymmetric unit of P22 procapsid Deposited 2023-01-13 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Chain G 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å
8U10 In situ cryo-EM structure of bacteriophage P22 gp1:gp4:gp5:gp10:gp9 N-term complex in conformation 1 at 3.2A resolution Deposited 2023-08-30 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Chain C 1–430（430 aa）
Chain D 1–430（430 aa）
Chain E 1–430（430 aa）
Chain F 1–430（430 aa）
Chain G 1–430（430 aa）
Chain H 1–430（430 aa）
Chain I 1–430（430 aa）
Chain J 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
9PGG Cryo-EM structure of bacteriophage P22 gp1-gp5-gp4 complex at 2.76 angstrom Deposited 2025-07-07 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 39 PDB declaration: 39-meric
Chain Aa 1–430（430 aa）
Chain Ab 1–430（430 aa）
Chain Ac 1–430（430 aa）
Chain Ad 1–430（430 aa）
Chain Ae 1–430（430 aa）
Chain Af 1–430（430 aa）
Chain Ag 1–430（430 aa）
Chain Ah 1–430（430 aa）
Chain Ai 1–430（430 aa）
Chain Aj 1–430（430 aa）
Chain Ak 1–430（430 aa）
Chain Al 1–430（430 aa）
Chain Am 1–430（430 aa）
Chain An 1–430（430 aa）
Chain Ao 1–430（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.76 Å

9 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

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.

SAXS scattering curve SAXS Profile

SAXS profile for 8u11

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8u11
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8u11
Deposition date deposition_date2023-08-30
Structure title titleIn 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 methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier86.11 Å
Radius of gyration Rg (electron density) rg_electron85.41 Å
Forward intensity I(0) i053703400000.00
Molecular weight molecular_weight1964600.0 kDa
Excluded volume excluded_volume2450600 ų
Envelope volume envelope_volume3684900 ų
Hydration-shell volume shell_volume333490 ų
Envelope diameter envelope_diameter265.4 Å
Shell Rg shell_rg95.77 Å
Envelope Rg envelope_rg83.54 Å
Shape Rg shape_rg85.41 Å
Total Rg total_rg85.48 Å
Total atoms total_atoms138386
Residues n_residues17588
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax295.2 Å
Rg (real space) rg_real87.74 Å
Rg uncertainty (real space) rg_real_error1.30 Å
I(0) (real space) i0_real5.3050e+10
I(0) uncertainty (real space) i0_real_error1.1140e+09
Rg (reciprocal space) rg_reciprocal87.95 Å
I(0) (reciprocal space) i0_reciprocal54000000000.0000
Solution quality estimate total_estimate0.9078
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary114.8 Å
Skewness Skewness skewness0.274
Kurtosis Kurtosis kurtosis-0.058
Angular range angular_range— – 0.0900 Å−1
Current regularization parameter α current_alpha1.2580
Highest regularization parameter α highest_alpha2644000000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.797; Stabil: 0.920; Sysdev: 1.000; Positv: 1.000; Valcen: 0.906; Smooth: 0.753
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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8. Citations (1)

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9. Files and Curves (10)