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9pgg

Cryo-EM structure of bacteriophage P22 gp1-gp5-gp4 complex at 2.76 angstrom

Method: ELECTRON MICROSCOPY Dmax: 298.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Major capsid protein

Salmonella phage P22

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 × 39 PDB declaration: 39-meric（39） Consistent with protein copy count Chain Aa； UniProt 1–430 Chain Ab； UniProt 1–430 Chain Ac； UniProt 1–430 Chain Ad； UniProt 1–430 Chain Ae； UniProt 1–430 Chain Af； UniProt 1–430 Chain Ag； UniProt 1–430 Chain Ah； UniProt 1–430 Chain Ai； UniProt 1–430 Chain Aj； UniProt 1–430 Chain Ak； UniProt 1–430 Chain Al； UniProt 1–430 Chain Am； UniProt 1–430 Chain An； UniProt 1–430 Chain Ao； UniProt 1–430 Not recorded Peptidoglycan hydrolase gp4 × 12 （P26746） Portal protein × 12 （P26744） ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.76 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 9PGG 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 construct Different mutation/modification Different oligomeric state 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
8U11 In situ cryo-EM structure of bacteriophage P22 gp1:gp5:gp4: gp10: gp9 N-term complex in conformation 2 at 3.1A resolution Deposited 2023-08-30 Different construct Different mutation/modification Different oligomeric state 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 3.10 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 1
Chains and sequence ranges Author chain Aa； PDBConstruct 1–430； UniProt 1–430 Author chain Ab； PDBConstruct 1–430； UniProt 1–430 Author chain Ac； PDBConstruct 1–430； UniProt 1–430 Author chain Ad； PDBConstruct 1–430； UniProt 1–430 Author chain Ae； PDBConstruct 1–430； UniProt 1–430 Author chain Af； PDBConstruct 1–430； UniProt 1–430 Author chain Ag； PDBConstruct 1–430； UniProt 1–430 Author chain Ah； PDBConstruct 1–430； UniProt 1–430 Author chain Ai； PDBConstruct 1–430； UniProt 1–430 Author chain Aj； PDBConstruct 1–430； UniProt 1–430 Author chain Ak； PDBConstruct 1–430； UniProt 1–430 Author chain Al； PDBConstruct 1–430； UniProt 1–430 Author chain Am； PDBConstruct 1–430； UniProt 1–430 Author chain An； PDBConstruct 1–430； UniProt 1–430 Author chain Ao； PDBConstruct 1–430； UniProt 1–430

Peptidoglycan hydrolase gp4

Salmonella phage P22

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 × 39 PDB declaration: 39-meric（39） Consistent with protein copy count Chain Ap； UniProt 1–166 Chain Aq； UniProt 1–166 Chain Ar； UniProt 1–166 Chain As； UniProt 1–166 Chain At； UniProt 1–166 Chain Au； UniProt 1–166 Chain Av； UniProt 1–166 Chain Aw； UniProt 1–166 Chain Ax； UniProt 1–166 Chain Ay； UniProt 1–166 Chain Az； UniProt 1–166 Chain Ba； UniProt 1–166 Not recorded Major capsid protein × 15 （P26747） Portal protein × 12 （P26744） ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.76 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 9PGG 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 oligomeric state 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
8U11 In situ cryo-EM structure of bacteriophage P22 gp1:gp5:gp4: gp10: gp9 N-term complex in conformation 2 at 3.1A resolution Deposited 2023-08-30 Different oligomeric state 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 3.10 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 2
Chains and sequence ranges Author chain Ap； PDBConstruct 1–166； UniProt 1–166 Author chain Aq； PDBConstruct 1–166； UniProt 1–166 Author chain Ar； PDBConstruct 1–166； UniProt 1–166 Author chain As； PDBConstruct 1–166； UniProt 1–166 Author chain At； PDBConstruct 1–166； UniProt 1–166 Author chain Au； PDBConstruct 1–166； UniProt 1–166 Author chain Av； PDBConstruct 1–166； UniProt 1–166 Author chain Aw； PDBConstruct 1–166； UniProt 1–166 Author chain Ax； PDBConstruct 1–166； UniProt 1–166 Author chain Ay； PDBConstruct 1–166； UniProt 1–166 Author chain Az； PDBConstruct 1–166； UniProt 1–166 Author chain Ba； PDBConstruct 1–166； UniProt 1–166

Portal protein

Salmonella phage P22

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 × 39 PDB declaration: 39-meric（39） Consistent with protein copy count Chain Bb； UniProt 1–725 Chain Bd； UniProt 1–725 Chain Bf； UniProt 1–725 Chain Bh； UniProt 1–725 Chain Bj； UniProt 1–725 Chain Bl； UniProt 1–725 Chain Bn； UniProt 1–725 Chain Bp； UniProt 1–725 Chain Br； UniProt 1–725 Chain Bt； UniProt 1–725 Chain Bv； UniProt 1–725 Chain Bx； UniProt 1–725 Not recorded Major capsid protein × 15 （P26747） Peptidoglycan hydrolase gp4 × 12 （P26746） ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.76 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 9PGG 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 oligomeric state 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
8U11 In situ cryo-EM structure of bacteriophage P22 gp1:gp5:gp4: gp10: gp9 N-term complex in conformation 2 at 3.1A resolution Deposited 2023-08-30 Different oligomeric state 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 3.10 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

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 Bb； PDBConstruct 1–725； UniProt 1–725 Author chain Bd； PDBConstruct 1–725； UniProt 1–725 Author chain Bf； PDBConstruct 1–725； UniProt 1–725 Author chain Bh； PDBConstruct 1–725； UniProt 1–725 Author chain Bj； PDBConstruct 1–725； UniProt 1–725 Author chain Bl； PDBConstruct 1–725； UniProt 1–725 Author chain Bn； PDBConstruct 1–725； UniProt 1–725 Author chain Bp； PDBConstruct 1–725； UniProt 1–725 Author chain Br； PDBConstruct 1–725； UniProt 1–725 Author chain Bt； PDBConstruct 1–725； UniProt 1–725 Author chain Bv； PDBConstruct 1–725； UniProt 1–725 Author chain Bx； PDBConstruct 1–725； UniProt 1–725

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 9pgg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9pgg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9pgg
Deposition date deposition_date2025-07-07
Structure title titleCryo-EM structure of bacteriophage P22 gp1-gp5-gp4 complex at 2.76 angstrom
Keywords keywordsPhage capsid-tail interface, VIRAL PROTEIN; 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_guinier81.51 Å
Radius of gyration Rg (electron density) rg_electron80.99 Å
Forward intensity I(0) i041107000000.00
Molecular weight molecular_weight1705200.0 kDa
Excluded volume excluded_volume2122500 ų
Envelope volume envelope_volume3274600 ų
Hydration-shell volume shell_volume312260 ų
Envelope diameter envelope_diameter309.1 Å
Shell Rg shell_rg93.08 Å
Envelope Rg envelope_rg80.48 Å
Shape Rg shape_rg80.96 Å
Total Rg total_rg81.19 Å
Total atoms total_atoms120038
Residues n_residues15287
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 dmax298.0 Å
Rg (real space) rg_real84.78 Å
Rg uncertainty (real space) rg_real_error1.82 Å
I(0) (real space) i0_real4.1090e+10
I(0) uncertainty (real space) i0_real_error8.3460e+08
Rg (reciprocal space) rg_reciprocal82.68 Å
I(0) (reciprocal space) i0_reciprocal41240000000.0000
Solution quality estimate total_estimate0.8801
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary109.8 Å
Skewness Skewness skewness0.528
Kurtosis Kurtosis kurtosis0.477
Angular range angular_range— – 0.0950 Å−1
Current regularization parameter α current_alpha0.9930
Highest regularization parameter α highest_alpha2871000000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.662; Stabil: 0.895; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.817
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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8. Citations (1)

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9. Files and Curves (10)