SAXSdb — 9ocl

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

Capsid protein VP1

OrganismNot specified

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 × 360 PDB declaration: 360-meric（360） Consistent with protein copy count	Chain 1； UniProt 579–879 Chain 2； UniProt 70–340	Not recorded	Capsid protein VP3 × 60 （A0A0K1U2R1） Capsid protein VP4 × 60 （D0QXH8） 10D2 Heavy Chain × 60 10D2 Light Chain × 60 PLM PALMITIC ACID × 60	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 Å
2	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain 1； UniProt 579–879 Chain 2； UniProt 70–340	Not recorded	Capsid protein VP3 × 1 （A0A0K1U2R1） Capsid protein VP4 × 1 （D0QXH8） 10D2 Heavy Chain × 1 10D2 Light Chain × 1 PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 Å
3	Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric（30） Consistent with protein copy count	Chain 1； UniProt 579–879 Chain 2； UniProt 70–340	Not recorded	Capsid protein VP3 × 5 （A0A0K1U2R1） Capsid protein VP4 × 5 （D0QXH8） 10D2 Heavy Chain × 5 10D2 Light Chain × 5 PLM PALMITIC ACID × 5	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 Å
4	Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric（36） Consistent with protein copy count	Chain 1； UniProt 579–879 Chain 2； UniProt 70–340	Not recorded	Capsid protein VP3 × 6 （A0A0K1U2R1） Capsid protein VP4 × 6 （D0QXH8） 10D2 Heavy Chain × 6 10D2 Light Chain × 6 PLM PALMITIC ACID × 6	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 Å
5	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain 1； UniProt 579–879 Chain 2； UniProt 70–340	Not recorded	Capsid protein VP3 × 1 （A0A0K1U2R1） Capsid protein VP4 × 1 （D0QXH8） 10D2 Heavy Chain × 1 10D2 Light Chain × 1 PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 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 9OCL	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1EAH PV2L COMPLEXED WITH ANTIVIRAL AGENT SCH48973 Deposited 1997-07-22	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 × 240 PDB declaration: 240-MERIC	Chain 1 578–878（301 aa） Chain 2 69–339（271 aa） Chain 3 340–577（238 aa） Chain 4 1–68（68 aa）	Not recorded	SC4 1[2-CHLORO-4-METHOXY-PHENYL-OXYMETHYL]-4-[2,6-DICHLORO-PHENYL-OXYMETHYL]-BENZENE × 60 MYR MYRISTIC ACID × 60	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.90 Å
1EAH PV2L COMPLEXED WITH ANTIVIRAL AGENT SCH48973 Deposited 1997-07-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain 1 578–878（301 aa） Chain 2 69–339（271 aa） Chain 3 340–577（238 aa） Chain 4 1–68（68 aa）	Not recorded	SC4 1[2-CHLORO-4-METHOXY-PHENYL-OXYMETHYL]-4-[2,6-DICHLORO-PHENYL-OXYMETHYL]-BENZENE × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.90 Å
1EAH PV2L COMPLEXED WITH ANTIVIRAL AGENT SCH48973 Deposited 1997-07-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	Chain 1 578–878（301 aa） Chain 2 69–339（271 aa） Chain 3 340–577（238 aa） Chain 4 1–68（68 aa）	Not recorded	SC4 1[2-CHLORO-4-METHOXY-PHENYL-OXYMETHYL]-4-[2,6-DICHLORO-PHENYL-OXYMETHYL]-BENZENE × 5 MYR MYRISTIC ACID × 5	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.90 Å
1EAH PV2L COMPLEXED WITH ANTIVIRAL AGENT SCH48973 Deposited 1997-07-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain 1 578–878（301 aa） Chain 2 69–339（271 aa） Chain 3 340–577（238 aa） Chain 4 1–68（68 aa）	Not recorded	SC4 1[2-CHLORO-4-METHOXY-PHENYL-OXYMETHYL]-4-[2,6-DICHLORO-PHENYL-OXYMETHYL]-BENZENE × 6 MYR MYRISTIC ACID × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.90 Å
1EAH PV2L COMPLEXED WITH ANTIVIRAL AGENT SCH48973 Deposited 1997-07-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain 1 578–878（301 aa） Chain 2 69–339（271 aa） Chain 3 340–577（238 aa） Chain 4 1–68（68 aa）	Not recorded	SC4 1[2-CHLORO-4-METHOXY-PHENYL-OXYMETHYL]-4-[2,6-DICHLORO-PHENYL-OXYMETHYL]-BENZENE × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.90 Å
1EAH PV2L COMPLEXED WITH ANTIVIRAL AGENT SCH48973 Deposited 1997-07-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 120 PDB declaration: 120-meric	Chain 1 578–878（301 aa） Chain 2 69–339（271 aa） Chain 3 340–577（238 aa） Chain 4 1–68（68 aa）	Not recorded	SC4 1[2-CHLORO-4-METHOXY-PHENYL-OXYMETHYL]-4-[2,6-DICHLORO-PHENYL-OXYMETHYL]-BENZENE × 30 MYR MYRISTIC ACID × 30	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.90 Å
3EPF CryoEM structure of poliovirus receptor bound to poliovirus type 2 Deposited 2008-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 300 PDB declaration: 300-MERIC	Chain 1 602–879（278 aa） Chain 2 79–340（262 aa） Chain 3 341–575（235 aa） Chain 4 2–69（68 aa）	Not recorded	SC4 1[2-CHLORO-4-METHOXY-PHENYL-OXYMETHYL]-4-[2,6-DICHLORO-PHENYL-OXYMETHYL]-BENZENE × 60 MYR MYRISTIC ACID × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.00 Å
3EPF CryoEM structure of poliovirus receptor bound to poliovirus type 2 Deposited 2008-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain 1 602–879（278 aa） Chain 2 79–340（262 aa） Chain 3 341–575（235 aa） Chain 4 2–69（68 aa）	Not recorded	SC4 1[2-CHLORO-4-METHOXY-PHENYL-OXYMETHYL]-4-[2,6-DICHLORO-PHENYL-OXYMETHYL]-BENZENE × 1 MYR MYRISTIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.00 Å
3EPF CryoEM structure of poliovirus receptor bound to poliovirus type 2 Deposited 2008-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 25 PDB declaration: 25-meric	Chain 1 602–879（278 aa） Chain 2 79–340（262 aa） Chain 3 341–575（235 aa） Chain 4 2–69（68 aa）	Not recorded	SC4 1[2-CHLORO-4-METHOXY-PHENYL-OXYMETHYL]-4-[2,6-DICHLORO-PHENYL-OXYMETHYL]-BENZENE × 5 MYR MYRISTIC ACID × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.00 Å
3EPF CryoEM structure of poliovirus receptor bound to poliovirus type 2 Deposited 2008-09-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain 1 602–879（278 aa） Chain 2 79–340（262 aa） Chain 3 341–575（235 aa） Chain 4 2–69（68 aa）	Not recorded	SC4 1[2-CHLORO-4-METHOXY-PHENYL-OXYMETHYL]-4-[2,6-DICHLORO-PHENYL-OXYMETHYL]-BENZENE × 6 MYR MYRISTIC ACID × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.00 Å
3EPF CryoEM structure of poliovirus receptor bound to poliovirus type 2 Deposited 2008-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain 1 602–879（278 aa） Chain 2 79–340（262 aa） Chain 3 341–575（235 aa） Chain 4 2–69（68 aa）	Not recorded	SC4 1[2-CHLORO-4-METHOXY-PHENYL-OXYMETHYL]-4-[2,6-DICHLORO-PHENYL-OXYMETHYL]-BENZENE × 1 MYR MYRISTIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.00 Å
8AYZ Poliovirus type 2 (strain MEF-1) virus-like particle in complex with capsid binder compound 17 Deposited 2022-09-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 180 PDB declaration: 180-meric	Chain A 579–879（301 aa） Chain B 1–340（340 aa） Chain C 342–578（237 aa）	Not recorded	SPH SPHINGOSINE × 60 FHK 4-[[4-[1,3-bis(oxidanylidene)isoindol-2-yl]phenyl]sulfonylamino]benzoic acid × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7；1 x DPBS was made from tissue culture grade Dulbecco's Phosphate Buffered Saline (Sigma-Aldrich). 20 mM EDTA was prepared from fresh stocks of buffered EDTA. cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；Single blotting with 3.5ul of sample. Four second blot time and -17 blot force on the vitrobot.	Resolution 1.88 Å
9F59 Poliovirus type 2 (strain MEF-1) stabilised virus-like particle (PV2 SC6b) from a mammalian expression system. Deposited 2024-04-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 180 PDB declaration: 180-meric	Chain A 579–879（301 aa） Chain B 2–340（339 aa） Chain C 341–578（238 aa）	Mutation：VP1 V107I, VP1 F134L, VP1 V183L Mutation：VP2 I57V, VP2 D126A Mutation：VP3 Q178L	SPH SPHINGOSINE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7；1 x DPBS, 20 mM EDTA, pH 7.0 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；4 ul of sample blotted for 3.5 seconds with -15 blot force on FEI Vitrobot mark IV.	Resolution 2.30 Å
9F5P Poliovirus type 2 (strain MEF-1) stabilised virus-like particle (PV2 SC6b) from an insect cell expression system. Deposited 2024-04-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 180 PDB declaration: 180-meric	Chain A 579–879（301 aa） Chain B 2–340（339 aa） Chain C 341–578（238 aa）	Mutation：VP1 V107I, VP1 V134L, VP1 V183L Mutation：VP2 I57V, VP2 D126A Mutation：VP3 Q178L	SPH SPHINGOSINE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7；1 x DPBS, 20 mM EDTA, pH 7.0 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；4 ul of sample blotted for 3.5 seconds with -15 blot force on FEI Vitrobot mark IV.	Resolution 2.60 Å
9H93 Poliovirus type 2 (strain MEF-1) stabilised virus-like particle (PV2 SC6b) from a yeast expression system. Deposited 2024-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 180 PDB declaration: 180-meric	Chain B 1–340（340 aa）	Mutation：VP4 I57V, VP2 D57A	SPH SPHINGOSINE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7；1 x DPBS, 20 mM EDTA, pH 7.0 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；3ul of sample double blotted for 3.5 seconds with -15 blot force on FEI Vitrobot mark IV.	Resolution 2.40 Å
9H94 Poliovirus type 2 (strain MEF-1) stabilised virus-like particle (PV2 SC5a) from a yeast expression system. Deposited 2024-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 180 PDB declaration: 180-meric	Chain B 1–340（340 aa）	Not recorded	SPH SPHINGOSINE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7；1 x DPBS, 20 mM EDTA, pH 7.0 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；3ul of sample double blotted for 3.5 seconds with -15 blot force on FEI Vitrobot mark IV.	Resolution 2.10 Å

7 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	POLG_POL2L
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain 1； PDBConstruct 1–301； UniProt 579–879 Author chain 2； PDBConstruct 1–271； UniProt 70–340

Capsid protein VP3

OrganismNot specified

UniProt A0A0K1U2R1

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 × 360 PDB declaration: 360-meric（360） Consistent with protein copy count	Chain 3； UniProt 341–575	Not recorded	Capsid protein VP1 × 60 （P06210） Capsid protein VP2 × 60 （P06210） Capsid protein VP4 × 60 （D0QXH8） 10D2 Heavy Chain × 60 10D2 Light Chain × 60 PLM PALMITIC ACID × 60	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 Å
2	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain 3； UniProt 341–575	Not recorded	Capsid protein VP1 × 1 （P06210） Capsid protein VP2 × 1 （P06210） Capsid protein VP4 × 1 （D0QXH8） 10D2 Heavy Chain × 1 10D2 Light Chain × 1 PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 Å
3	Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric（30） Consistent with protein copy count	Chain 3； UniProt 341–575	Not recorded	Capsid protein VP1 × 5 （P06210） Capsid protein VP2 × 5 （P06210） Capsid protein VP4 × 5 （D0QXH8） 10D2 Heavy Chain × 5 10D2 Light Chain × 5 PLM PALMITIC ACID × 5	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 Å
4	Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric（36） Consistent with protein copy count	Chain 3； UniProt 341–575	Not recorded	Capsid protein VP1 × 6 （P06210） Capsid protein VP2 × 6 （P06210） Capsid protein VP4 × 6 （D0QXH8） 10D2 Heavy Chain × 6 10D2 Light Chain × 6 PLM PALMITIC ACID × 6	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 Å
5	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain 3； UniProt 341–575	Not recorded	Capsid protein VP1 × 1 （P06210） Capsid protein VP2 × 1 （P06210） Capsid protein VP4 × 1 （D0QXH8） 10D2 Heavy Chain × 1 10D2 Light Chain × 1 PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 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 9OCL	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8E8S 9H2 Fab-poliovirus 2 complex Deposited 2022-08-25	Different construct Different mutation/modification Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 360 PDB declaration: 360-meric	Chain 2 79–340（262 aa） Chain 3 341–575（235 aa）	Not recorded	PLM PALMITIC ACID × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.73 Å
8E8S 9H2 Fab-poliovirus 2 complex Deposited 2022-08-25	Different construct Different mutation/modification Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain 2 79–340（262 aa） Chain 3 341–575（235 aa）	Not recorded	PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.73 Å
8E8S 9H2 Fab-poliovirus 2 complex Deposited 2022-08-25	Different construct Different mutation/modification Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain 2 79–340（262 aa） Chain 3 341–575（235 aa）	Not recorded	PLM PALMITIC ACID × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.73 Å
8E8S 9H2 Fab-poliovirus 2 complex Deposited 2022-08-25	Different construct Different mutation/modification Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 2 79–340（262 aa） Chain 3 341–575（235 aa）	Not recorded	PLM PALMITIC ACID × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.73 Å
8E8S 9H2 Fab-poliovirus 2 complex Deposited 2022-08-25	Different construct Different mutation/modification Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain 2 79–340（262 aa） Chain 3 341–575（235 aa）	Not recorded	PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.73 Å
9H93 Poliovirus type 2 (strain MEF-1) stabilised virus-like particle (PV2 SC6b) from a yeast expression system. Deposited 2024-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 180 PDB declaration: 180-meric	Chain C 341–578（238 aa）	Mutation：VP3 Q178L	SPH SPHINGOSINE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7；1 x DPBS, 20 mM EDTA, pH 7.0 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；3ul of sample double blotted for 3.5 seconds with -15 blot force on FEI Vitrobot mark IV.	Resolution 2.40 Å
9H94 Poliovirus type 2 (strain MEF-1) stabilised virus-like particle (PV2 SC5a) from a yeast expression system. Deposited 2024-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 180 PDB declaration: 180-meric	Chain C 341–578（238 aa）	Mutation：VP3 L85F, VP3 Q178L	SPH SPHINGOSINE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7；1 x DPBS, 20 mM EDTA, pH 7.0 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；3ul of sample double blotted for 3.5 seconds with -15 blot force on FEI Vitrobot mark IV.	Resolution 2.10 Å

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

View Construct and Data Evidence

UniProt name	A0A0K1U2R1_9ENTO
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain 3； PDBConstruct 1–235； UniProt 341–575

Capsid protein VP4

OrganismNot specified

UniProt D0QXH8

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 × 360 PDB declaration: 360-meric（360） Consistent with protein copy count	Chain 4； UniProt 2–69	Not recorded	Capsid protein VP1 × 60 （P06210） Capsid protein VP2 × 60 （P06210） Capsid protein VP3 × 60 （A0A0K1U2R1） 10D2 Heavy Chain × 60 10D2 Light Chain × 60 PLM PALMITIC ACID × 60	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 Å
2	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain 4； UniProt 2–69	Not recorded	Capsid protein VP1 × 1 （P06210） Capsid protein VP2 × 1 （P06210） Capsid protein VP3 × 1 （A0A0K1U2R1） 10D2 Heavy Chain × 1 10D2 Light Chain × 1 PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 Å
3	Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric（30） Consistent with protein copy count	Chain 4； UniProt 2–69	Not recorded	Capsid protein VP1 × 5 （P06210） Capsid protein VP2 × 5 （P06210） Capsid protein VP3 × 5 （A0A0K1U2R1） 10D2 Heavy Chain × 5 10D2 Light Chain × 5 PLM PALMITIC ACID × 5	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 Å
4	Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric（36） Consistent with protein copy count	Chain 4； UniProt 2–69	Not recorded	Capsid protein VP1 × 6 （P06210） Capsid protein VP2 × 6 （P06210） Capsid protein VP3 × 6 （A0A0K1U2R1） 10D2 Heavy Chain × 6 10D2 Light Chain × 6 PLM PALMITIC ACID × 6	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 Å
5	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain 4； UniProt 2–69	Not recorded	Capsid protein VP1 × 1 （P06210） Capsid protein VP2 × 1 （P06210） Capsid protein VP3 × 1 （A0A0K1U2R1） 10D2 Heavy Chain × 1 10D2 Light Chain × 1 PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.65 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 9OCL	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8E8S 9H2 Fab-poliovirus 2 complex Deposited 2022-08-25	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 360 PDB declaration: 360-meric	Chain 4 2–69（68 aa）	Not recorded	PLM PALMITIC ACID × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.73 Å
8E8S 9H2 Fab-poliovirus 2 complex Deposited 2022-08-25	Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain 4 2–69（68 aa）	Not recorded	PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.73 Å
8E8S 9H2 Fab-poliovirus 2 complex Deposited 2022-08-25	Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain 4 2–69（68 aa）	Not recorded	PLM PALMITIC ACID × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.73 Å
8E8S 9H2 Fab-poliovirus 2 complex Deposited 2022-08-25	Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 4 2–69（68 aa）	Not recorded	PLM PALMITIC ACID × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.73 Å
8E8S 9H2 Fab-poliovirus 2 complex Deposited 2022-08-25	Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain 4 2–69（68 aa）	Not recorded	PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.73 Å

1 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	D0QXH8_9ENTO
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain 4； PDBConstruct 1–68； UniProt 2–69

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9ocl
Deposition date deposition_date	2025-04-24
Structure title title	PV2-10D2 Complex
Keywords keywords	Virus, Antibody, Complex; VIRUS
Experimental Method method	ELECTRON MICROSCOPY

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	34.73 Å
Radius of gyration Rg (electron density) rg_electron	33.92 Å
Forward intensity I(0) i0	217769000.00
Molecular weight molecular_weight	117470.0 kDa
Excluded volume excluded_volume	146640 Å³
Envelope volume envelope_volume	208920 Å³
Hydration-shell volume shell_volume	50669 Å³
Envelope diameter envelope_diameter	117.4 Å
Shell Rg shell_rg	41.18 Å
Envelope Rg envelope_rg	33.84 Å
Shape Rg shape_rg	33.88 Å
Total Rg total_rg	34.62 Å
Total atoms total_atoms	16318
Residues n_residues	1065
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	110.4 Å
Rg (real space) rg_real	34.63 Å
Rg uncertainty (real space) rg_real_error	0.63 Å
I(0) (real space) i0_real	2.1780e+08
I(0) uncertainty (real space) i0_real_error	3.5330e+06
Rg (reciprocal space) rg_reciprocal	34.69 Å
I(0) (reciprocal space) i0_reciprocal	217800000.0000
Solution quality estimate total_estimate	0.8996
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	40.8 Å
Skewness Skewness skewness	0.229
Kurtosis Kurtosis kurtosis	-0.512
Angular range angular_range	— – 0.2300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	55240000.0000
Real-space data points n_real_points	47
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.928; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.912

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	Capsid protein VP1
Molecular weight formula_weight	33039.1 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1
Atom count atom_count	16318

GLGDLIEGVVEGVTRNALTPLTPANNLPDTQSSGPAHSKETPALTAVETGATNPLVPSDTVQTRHVIQKRTRSESTVESFFARGACVAIIEVDNDAPTKRASKLFSVWKITYKDTVQLRRKLEFFTYSRFDMEFTFVVTSNYTDANNGHALNQVYQIMYIPPGAPIPGKWNDYTWQTSSNPSVFYTYGAPPARISVPYVGIANAYSHFYDGFAKVPLAGQASTEGDSLYGAASLNDFGSLAVRVVNDHNPTKLTSKIRVYMKPKHVRVWCPRPPRAVPYYGPGVDYKDGLAPLPGKGLTTY

Entity 2 Entity 2 polymer

Description description	Capsid protein VP2
Molecular weight formula_weight	29980.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	2

SPNIEACGYSVRVMQLTLGNSTITTQEAANSVVAYGRWPEYIKDSEANPVDQPTEPDVAACRFYTLDTVTWRKESRGWWWKLPDALKDMGLFGQNMFYHYLGRAGYTVHVQCNASKFHQGALGVFAVPEMCLAGDSTTHMFTKYENANPGEKGGEFKGSFTLDTNATNPARNFCPVDYLFGSGVLAGNAFVYPHQIINLRTNNCATLVLPYVNSLSIDSMTKHNNWGIAILPLAPLDFATESSTEIPITLTIAPMCCEFNGLRNITVPRTQ

Entity 3 Entity 3 polymer

Description description	Capsid protein VP3
Molecular weight formula_weight	26115.9 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	3

GLPVLNTPGSNQYLTADNYQSPCAIPEFDVTPPIDIPGEVRNMMELAEIDTMIPLNLTNQRKNTMDMYRVELNDAAHSDTPILCLSLSPASDPRLAHTMLGEILNYYTHWAGSLKFTFLFCGSMMATGKLLVSYAPPGAEAPKSRKEAMLGTHVIWDIGLQSSCTMVVPWISNTTYRQTINDSFTEGGYISMFYQTRVVVPLSTPRKMDILGFVSACNDFSVRLLRDTTHISQEA

Entity 4 Entity 4 polymer

Description description	Capsid protein VP4
Molecular weight formula_weight	7347.0 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	4

GAQVSSQKVGAHENSNRAYGGSTINYTTINYYRDSASNAASKQDFAQDPSKFTEPIKDVLIKTAPTLN

Entity 5 Entity 5 polymer

Description description	10D2 Heavy Chain
Molecular weight formula_weight	14713.2 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

QVQLQQSGPGLVKPSETLSLTCAISGDSVSSKSAAWNWIRQSPSRGLEWLGRTYYRSKWSHNYAVSVRSRVTINPDTSKNQFSLHLNSVTPEDTAVYYCTRASPSAYTHGWYGSYYYGMDVWGQGTTVTVSS

Entity 6 Entity 6 polymer

Description description	10D2 Light Chain
Molecular weight formula_weight	11453.5 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L

QSALTQPASVSGSPGQSITISCTGSSSDISDYNYVAWYQQHPGKAPKLIISDVSIRPSGVSARFSGSKSGNTASLTISGLQVEDEADYYCSSYTSDINILFGGGTKLTVL

Entity 7 Entity 7 non-polymer

Description description	PALMITIC ACID
Molecular weight formula_weight	256.4 kDa
Source method src_method	syn
Copy count entity_count	1

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

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

Resolution resolution	3.650 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	3.65 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	21606

fit	/app/data/saxs_computation/oc/9ocl/9ocl.fit
pddf	/app/data/pr_computation/oc/9ocl/9ocl.pr.out
profile	/app/data/saxs_computation/oc/9ocl/9ocl.dat

PV2-10D2 Complex

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

Capsid protein VP1

State in the Current Structure

Other States of the Same Protein in the Database

Capsid protein VP3

State in the Current Structure

Other States of the Same Protein in the Database

Capsid protein VP4

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

Entity 6 Entity 6 polymer

Polymer Polymer

Entity 7 Entity 7 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)