Current Protein Identity:P26744
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Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 3LJ5 Full Length Bacteriophage P22 Portal Protein Deposited 2010-01-25 | Assembly 1 Protein homooligomer Homooligomer;Protein × 12 PDB declaration: dodecameric(12) Consistent with protein count |
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 | Assembly 1 Protein heterocomplex Heteromer;Protein × 24 PDB declaration: 24-meric(24) Consistent with protein count |
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 | Assembly 2 Protein heterocomplex Heteromer;Protein × 24 PDB declaration: 24-meric(24) Consistent with protein count |
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 | Assembly 1 Protein heterocomplex Heteromer;Protein × 27 PDB declaration: 27-meric(27) Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer;Protein × 12 PDB declaration: dodecameric(12) Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer;Protein × 12 PDB declaration: dodecameric(12) Consistent with protein count |
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 | Assembly 1 Protein heterocomplex Heteromer;Protein × 24 PDB declaration: 24-meric(24) Consistent with protein count |
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 | Assembly 1 Protein heterocomplex Heteromer;Protein × 24 PDB declaration: 24-meric(24) Consistent with protein count |
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 | Assembly 1 Protein heterocomplex Heteromer;Protein × 58 PDB declaration: 58-meric(58) Consistent with protein count |
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 | Assembly 1 Protein heterocomplex Heteromer;Protein × 58 PDB declaration: 58-meric(58) Consistent with protein count |
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 | Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer;Protein × 12 PDB declaration: 12-meric(12) Consistent with protein count |
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 | Assembly 1 Protein heterocomplex Heteromer;Protein × 39 PDB declaration: 39-meric(39) Consistent with protein count |
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 |