SAXSdb — 7tnq

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

Microtubule associated protein SPM1

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 × 100 PDB declaration: 100-meric（100） Consistent with protein copy count	Chain 0； UniProt 1–351 Chain 1； UniProt 1–351 Chain 10； UniProt 1–351 Chain 11； UniProt 1–351 Chain 12； UniProt 1–351 Chain 13； UniProt 1–351 Chain 14； UniProt 1–351 Chain 15； UniProt 1–351 Chain 16； UniProt 1–351 Chain 17； UniProt 1–351 Chain 18； UniProt 1–351 Chain 19； UniProt 1–351 Chain 2； UniProt 1–351 Chain 20； UniProt 1–351 Chain 21； UniProt 1–351 Chain 22； UniProt 1–351 Chain 23； UniProt 1–351 Chain 3； UniProt 1–351 Chain 4； UniProt 1–351 Chain 5； UniProt 1–351 Chain 6； UniProt 1–351 Chain 7； UniProt 1–351 Chain 8； UniProt 1–351 Chain 9； UniProt 1–351	Not recorded	Tubulin alpha chain × 26 （P10873） Tubulin beta chain × 26 （A0A125YWG5） PDI family protein × 20 （A0A125YMM3） PDI family protein × 4 （A0A125YFI4）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.2；Phosphate Buffered Saline cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 8.40 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 7TNQ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7TNS Subpellicular microtubule from detergent-extract Toxoplasma gondii cells Deposited 2022-01-21	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 101 PDB declaration: 101-meric	Chain 0 1–351（351 aa） Chain 1 1–351（351 aa） Chain 10 1–351（351 aa） Chain 11 1–351（351 aa） Chain 12 1–351（351 aa） Chain 13 1–351（351 aa） Chain 14 1–351（351 aa） Chain 15 1–351（351 aa） Chain 16 1–351（351 aa） Chain 17 1–351（351 aa） Chain 18 1–351（351 aa） Chain 19 1–351（351 aa） Chain 2 1–351（351 aa） Chain 20 1–351（351 aa） Chain 21 1–351（351 aa） Chain 22 1–351（351 aa） Chain 23 1–351（351 aa） Chain 3 1–351（351 aa） Chain 4 1–351（351 aa） Chain 5 1–351（351 aa） Chain 6 1–351（351 aa） Chain 7 1–351（351 aa） Chain 8 1–351（351 aa） Chain 9 1–351（351 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Phosphate-Buffered Saline cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.70 Å

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

View Construct and Data Evidence

UniProt name	S8F1Y1_TOXGM
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 0； PDBConstruct 1–351； UniProt 1–351 Author chain 1； PDBConstruct 1–351； UniProt 1–351 Author chain 10； PDBConstruct 1–351； UniProt 1–351 Author chain 11； PDBConstruct 1–351； UniProt 1–351 Author chain 12； PDBConstruct 1–351； UniProt 1–351 Author chain 13； PDBConstruct 1–351； UniProt 1–351 Author chain 14； PDBConstruct 1–351； UniProt 1–351 Author chain 15； PDBConstruct 1–351； UniProt 1–351 Author chain 16； PDBConstruct 1–351； UniProt 1–351 Author chain 17； PDBConstruct 1–351； UniProt 1–351 Author chain 18； PDBConstruct 1–351； UniProt 1–351 Author chain 19； PDBConstruct 1–351； UniProt 1–351 Author chain 2； PDBConstruct 1–351； UniProt 1–351 Author chain 20； PDBConstruct 1–351； UniProt 1–351 Author chain 21； PDBConstruct 1–351； UniProt 1–351 Author chain 22； PDBConstruct 1–351； UniProt 1–351 Author chain 23； PDBConstruct 1–351； UniProt 1–351 Author chain 3； PDBConstruct 1–351； UniProt 1–351 Author chain 4； PDBConstruct 1–351； UniProt 1–351 Author chain 5； PDBConstruct 1–351； UniProt 1–351 Author chain 6； PDBConstruct 1–351； UniProt 1–351 Author chain 7； PDBConstruct 1–351； UniProt 1–351 Author chain 8； PDBConstruct 1–351； UniProt 1–351 Author chain 9； PDBConstruct 1–351； UniProt 1–351

Tubulin alpha chain

OrganismNot specified

UniProt P10873

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 × 100 PDB declaration: 100-meric（100） Consistent with protein copy count	Chain A0； UniProt 1–453 Chain A2； UniProt 1–453 Chain A4； UniProt 1–453 Chain A6； UniProt 1–453 Chain A8； UniProt 1–453 Chain B0； UniProt 1–453 Chain B2； UniProt 1–453 Chain B4； UniProt 1–453 Chain B6； UniProt 1–453 Chain B8； UniProt 1–453 Chain C0； UniProt 1–453 Chain C2； UniProt 1–453 Chain C4； UniProt 1–453 Chain C6； UniProt 1–453 Chain C8； UniProt 1–453 Chain D0； UniProt 1–453 Chain D2； UniProt 1–453 Chain D4； UniProt 1–453 Chain D6； UniProt 1–453 Chain D8； UniProt 1–453 Chain E0； UniProt 1–453 Chain E2； UniProt 1–453 Chain E4； UniProt 1–453 Chain E6； UniProt 1–453 Chain E8； UniProt 1–453 Chain F0； UniProt 1–453	Not recorded	Microtubule associated protein SPM1 × 24 （S8F1Y1） Tubulin beta chain × 26 （A0A125YWG5） PDI family protein × 20 （A0A125YMM3） PDI family protein × 4 （A0A125YFI4）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.2；Phosphate Buffered Saline cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 8.40 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 7TNQ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7MIZ Atomic structure of cortical microtubule from Toxoplasma gondii Deposited 2021-04-18	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 100 PDB declaration: 100-meric	Chain A0 1–453（453 aa） Chain A2 1–453（453 aa） Chain A4 1–453（453 aa） Chain A6 1–453（453 aa） Chain A8 1–453（453 aa） Chain B0 1–453（453 aa） Chain B2 1–453（453 aa） Chain B4 1–453（453 aa） Chain B6 1–453（453 aa） Chain B8 1–453（453 aa） Chain C0 1–453（453 aa） Chain C2 1–453（453 aa） Chain C4 1–453（453 aa） Chain C6 1–453（453 aa） Chain C8 1–453（453 aa） Chain D0 1–453（453 aa） Chain D2 1–453（453 aa） Chain D4 1–453（453 aa） Chain D6 1–453（453 aa） Chain D8 1–453（453 aa） Chain E0 1–453（453 aa） Chain E2 1–453（453 aa） Chain E4 1–453（453 aa） Chain E6 1–453（453 aa） Chain E8 1–453（453 aa） Chain F0 1–453（453 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 26 MG MAGNESIUM ION × 26 GDP GUANOSINE-5'-DIPHOSPHATE × 26	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；blot for 4 seconds with a blot force of -15	Resolution 3.40 Å
7TNS Subpellicular microtubule from detergent-extract Toxoplasma gondii cells Deposited 2022-01-21	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 101 PDB declaration: 101-meric	Chain A0 1–453（453 aa） Chain A2 1–453（453 aa） Chain A4 1–453（453 aa） Chain A6 1–453（453 aa） Chain A8 1–453（453 aa） Chain B0 1–453（453 aa） Chain B2 1–453（453 aa） Chain B4 1–453（453 aa） Chain B6 1–453（453 aa） Chain B8 1–453（453 aa） Chain C0 1–453（453 aa） Chain C2 1–453（453 aa） Chain C4 1–453（453 aa） Chain C6 1–453（453 aa） Chain C8 1–453（453 aa） Chain D0 1–453（453 aa） Chain D2 1–453（453 aa） Chain D4 1–453（453 aa） Chain D6 1–453（453 aa） Chain D8 1–453（453 aa） Chain E0 1–453（453 aa） Chain E2 1–453（453 aa） Chain E4 1–453（453 aa） Chain E6 1–453（453 aa） Chain E8 1–453（453 aa） Chain F0 1–453（453 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Phosphate-Buffered Saline cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.70 Å
7TNT The tubulin-based conoid from detergent-extract Toxoplasma gondii cells Deposited 2022-01-21	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 2A 1–437（437 aa） Chain 2B 1–437（437 aa） Chain 2C 1–437（437 aa） Chain 2D 1–437（437 aa） Chain 2E 1–437（437 aa） Chain 2F 1–437（437 aa） Chain 2G 1–437（437 aa） Chain 2H 1–437（437 aa） Chain 2I 1–437（437 aa） Chain 4A 1–437（437 aa） Chain 4B 1–437（437 aa） Chain 4C 1–437（437 aa） Chain 4D 1–437（437 aa） Chain 4E 1–437（437 aa） Chain 4F 1–437（437 aa） Chain 4G 1–437（437 aa） Chain 4H 1–437（437 aa） Chain 4I 1–437（437 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Phosphate Buffered Saline cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.30 Å
9Y9Z Cryo-EM structure of conoid fiber from Toxoplasma gondii (24-nm repeat) Deposited 2025-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 378 PDB declaration: 378-meric	Chain 1A 1–453（453 aa） Chain 1C 1–453（453 aa） Chain 1E 1–453（453 aa） Chain 1G 1–453（453 aa） Chain 1I 1–453（453 aa） Chain 1K 1–453（453 aa） Chain 1M 1–453（453 aa） Chain 2A 1–453（453 aa） Chain 2C 1–453（453 aa） Chain 2E 1–453（453 aa） Chain 2G 1–453（453 aa） Chain 2I 1–453（453 aa） Chain 2K 1–453（453 aa） Chain 2M 1–453（453 aa） Chain 3A 1–453（453 aa） Chain 3C 1–453（453 aa） Chain 3E 1–453（453 aa） Chain 3G 1–453（453 aa） Chain 3I 1–453（453 aa） Chain 3K 1–453（453 aa） Chain 3M 1–453（453 aa） Chain 4A 1–453（453 aa） Chain 4C 1–453（453 aa） Chain 4E 1–453（453 aa） Chain 4G 1–453（453 aa） Chain 4I 1–453（453 aa） Chain 4K 1–453（453 aa） Chain 4M 1–453（453 aa） Chain 5A 1–453（453 aa） Chain 5C 1–453（453 aa） Chain 5E 1–453（453 aa） Chain 5G 1–453（453 aa） Chain 5I 1–453（453 aa） Chain 5K 1–453（453 aa） Chain 5M 1–453（453 aa） Chain 6A 1–453（453 aa） Chain 6C 1–453（453 aa） Chain 6E 1–453（453 aa） Chain 6G 1–453（453 aa） Chain 6I 1–453（453 aa） Chain 6K 1–453（453 aa） Chain 6M 1–453（453 aa） Chain 7A 1–453（453 aa） Chain 7C 1–453（453 aa） Chain 7E 1–453（453 aa） Chain 7G 1–453（453 aa） Chain 7I 1–453（453 aa） Chain 7K 1–453（453 aa） Chain 7M 1–453（453 aa） Chain 8A 1–453（453 aa） Chain 8C 1–453（453 aa） Chain 8E 1–453（453 aa） Chain 8G 1–453（453 aa） Chain 8I 1–453（453 aa） Chain 8K 1–453（453 aa） Chain 8M 1–453（453 aa） Chain 9A 1–453（453 aa） Chain 9C 1–453（453 aa） Chain 9E 1–453（453 aa） Chain 9G 1–453（453 aa） Chain 9I 1–453（453 aa） Chain 9K 1–453（453 aa） Chain 9M 1–453（453 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 63 MG MAGNESIUM ION × 54 GDP GUANOSINE-5'-DIPHOSPHATE × 57	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.14 Å
9YA1 Cryo-EM structure of intraconoidal microtubule 2 (ICMT2) from Toxoplasma gondii (8-nm repeat) Deposited 2025-09-15	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 96 PDB declaration: 96-meric	Chain A0 1–453（453 aa） Chain A2 1–453（453 aa） Chain A4 1–453（453 aa） Chain A6 1–453（453 aa） Chain A8 1–453（453 aa） Chain B0 1–453（453 aa） Chain B2 1–453（453 aa） Chain B4 1–453（453 aa） Chain B6 1–453（453 aa） Chain B8 1–453（453 aa） Chain C0 1–453（453 aa） Chain C2 1–453（453 aa） Chain C4 1–453（453 aa） Chain C6 1–453（453 aa） Chain C8 1–453（453 aa） Chain D0 1–453（453 aa） Chain D2 1–453（453 aa） Chain D4 1–453（453 aa） Chain D6 1–453（453 aa） Chain D8 1–453（453 aa） Chain E0 1–453（453 aa） Chain E2 1–453（453 aa） Chain E4 1–453（453 aa） Chain E6 1–453（453 aa） Chain E8 1–453（453 aa） Chain F0 1–453（453 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 26 MG MAGNESIUM ION × 26 GDP GUANOSINE-5'-DIPHOSPHATE × 26	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.52 Å
9YA2 Cryo-EM structure of intraconoidal microtubule 1 (ICMT1) from Toxoplasma gondii (8-nm repeat) Deposited 2025-09-15	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 99 PDB declaration: 99-meric	Chain A0 1–453（453 aa） Chain A2 1–453（453 aa） Chain A4 1–453（453 aa） Chain A6 1–453（453 aa） Chain A8 1–453（453 aa） Chain B0 1–453（453 aa） Chain B2 1–453（453 aa） Chain B4 1–453（453 aa） Chain B6 1–453（453 aa） Chain B8 1–453（453 aa） Chain C0 1–453（453 aa） Chain C2 1–453（453 aa） Chain C4 1–453（453 aa） Chain C6 1–453（453 aa） Chain C8 1–453（453 aa） Chain D0 1–453（453 aa） Chain D2 1–453（453 aa） Chain D4 1–453（453 aa） Chain D6 1–453（453 aa） Chain D8 1–453（453 aa） Chain E0 1–453（453 aa） Chain E2 1–453（453 aa） Chain E4 1–453（453 aa） Chain E6 1–453（453 aa） Chain E8 1–453（453 aa） Chain F0 1–453（453 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 26 MG MAGNESIUM ION × 26 GDP GUANOSINE-5'-DIPHOSPHATE × 26	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.34 Å
9YA3 Cryo-EM structure of the apical region of subpellicular microtubule (SPMT) from Toxoplasma gondii (8-nm repeat) Deposited 2025-09-15	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 108 PDB declaration: 108-meric	Chain A0 1–453（453 aa） Chain A2 1–453（453 aa） Chain A4 1–453（453 aa） Chain A6 1–453（453 aa） Chain A8 1–453（453 aa） Chain B0 1–453（453 aa） Chain B2 1–453（453 aa） Chain B4 1–453（453 aa） Chain B6 1–453（453 aa） Chain B8 1–453（453 aa） Chain C0 1–453（453 aa） Chain C2 1–453（453 aa） Chain C4 1–453（453 aa） Chain C6 1–453（453 aa） Chain C8 1–453（453 aa） Chain D0 1–453（453 aa） Chain D2 1–453（453 aa） Chain D4 1–453（453 aa） Chain D6 1–453（453 aa） Chain D8 1–453（453 aa） Chain E0 1–453（453 aa） Chain E2 1–453（453 aa） Chain E4 1–453（453 aa） Chain E6 1–453（453 aa） Chain E8 1–453（453 aa） Chain F0 1–453（453 aa）	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 26 GTP GUANOSINE-5'-TRIPHOSPHATE × 26 MG MAGNESIUM ION × 26	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å

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

View Construct and Data Evidence

UniProt name	TBA_TOXGO
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A0； PDBConstruct 1–453； UniProt 1–453 Author chain A2； PDBConstruct 1–453； UniProt 1–453 Author chain A4； PDBConstruct 1–453； UniProt 1–453 Author chain A6； PDBConstruct 1–453； UniProt 1–453 Author chain A8； PDBConstruct 1–453； UniProt 1–453 Author chain B0； PDBConstruct 1–453； UniProt 1–453 Author chain B2； PDBConstruct 1–453； UniProt 1–453 Author chain B4； PDBConstruct 1–453； UniProt 1–453 Author chain B6； PDBConstruct 1–453； UniProt 1–453 Author chain B8； PDBConstruct 1–453； UniProt 1–453 Author chain C0； PDBConstruct 1–453； UniProt 1–453 Author chain C2； PDBConstruct 1–453； UniProt 1–453 Author chain C4； PDBConstruct 1–453； UniProt 1–453 Author chain C6； PDBConstruct 1–453； UniProt 1–453 Author chain C8； PDBConstruct 1–453； UniProt 1–453 Author chain D0； PDBConstruct 1–453； UniProt 1–453 Author chain D2； PDBConstruct 1–453； UniProt 1–453 Author chain D4； PDBConstruct 1–453； UniProt 1–453 Author chain D6； PDBConstruct 1–453； UniProt 1–453 Author chain D8； PDBConstruct 1–453； UniProt 1–453 Author chain E0； PDBConstruct 1–453； UniProt 1–453 Author chain E2； PDBConstruct 1–453； UniProt 1–453 Author chain E4； PDBConstruct 1–453； UniProt 1–453 Author chain E6； PDBConstruct 1–453； UniProt 1–453 Author chain E8； PDBConstruct 1–453； UniProt 1–453 Author chain F0； PDBConstruct 1–453； UniProt 1–453

Tubulin beta chain

OrganismNot specified

UniProt A0A125YWG5

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 × 100 PDB declaration: 100-meric（100） Consistent with protein copy count	Chain A1； UniProt 1–449 Chain A3； UniProt 1–449 Chain A5； UniProt 1–449 Chain A7； UniProt 1–449 Chain A9； UniProt 1–449 Chain B1； UniProt 1–449 Chain B3； UniProt 1–449 Chain B5； UniProt 1–449 Chain B7； UniProt 1–449 Chain B9； UniProt 1–449 Chain C1； UniProt 1–449 Chain C3； UniProt 1–449 Chain C5； UniProt 1–449 Chain C7； UniProt 1–449 Chain C9； UniProt 1–449 Chain D1； UniProt 1–449 Chain D3； UniProt 1–449 Chain D5； UniProt 1–449 Chain D7； UniProt 1–449 Chain D9； UniProt 1–449 Chain E1； UniProt 1–449 Chain E3； UniProt 1–449 Chain E5； UniProt 1–449 Chain E7； UniProt 1–449 Chain E9； UniProt 1–449 Chain F1； UniProt 1–449	Not recorded	Microtubule associated protein SPM1 × 24 （S8F1Y1） Tubulin alpha chain × 26 （P10873） PDI family protein × 20 （A0A125YMM3） PDI family protein × 4 （A0A125YFI4）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.2；Phosphate Buffered Saline cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 8.40 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 7TNQ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7TNS Subpellicular microtubule from detergent-extract Toxoplasma gondii cells Deposited 2022-01-21	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 101 PDB declaration: 101-meric	Chain A1 1–449（449 aa） Chain A3 1–449（449 aa） Chain A5 1–449（449 aa） Chain A7 1–449（449 aa） Chain A9 1–449（449 aa） Chain B1 1–449（449 aa） Chain B3 1–449（449 aa） Chain B5 1–449（449 aa） Chain B7 1–449（449 aa） Chain B9 1–449（449 aa） Chain C1 1–449（449 aa） Chain C3 1–449（449 aa） Chain C5 1–449（449 aa） Chain C7 1–449（449 aa） Chain C9 1–449（449 aa） Chain D1 1–449（449 aa） Chain D3 1–449（449 aa） Chain D5 1–449（449 aa） Chain D7 1–449（449 aa） Chain D9 1–449（449 aa） Chain E1 1–449（449 aa） Chain E3 1–449（449 aa） Chain E5 1–449（449 aa） Chain E7 1–449（449 aa） Chain E9 1–449（449 aa） Chain F1 1–449（449 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Phosphate-Buffered Saline cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.70 Å
7TNT The tubulin-based conoid from detergent-extract Toxoplasma gondii cells Deposited 2022-01-21	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 3A 1–426（426 aa） Chain 3B 1–426（426 aa） Chain 3C 1–426（426 aa） Chain 3D 1–426（426 aa） Chain 3E 1–426（426 aa） Chain 3F 1–426（426 aa） Chain 3G 1–426（426 aa） Chain 3H 1–426（426 aa） Chain 3I 1–426（426 aa） Chain 5A 1–426（426 aa） Chain 5B 1–426（426 aa） Chain 5C 1–426（426 aa） Chain 5D 1–426（426 aa） Chain 5E 1–426（426 aa） Chain 5F 1–426（426 aa） Chain 5G 1–426（426 aa） Chain 5H 1–426（426 aa） Chain 5I 1–426（426 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Phosphate Buffered Saline cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.30 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A125YWG5_TOXGM
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain A1； PDBConstruct 1–449； UniProt 1–449 Author chain A3； PDBConstruct 1–449； UniProt 1–449 Author chain A5； PDBConstruct 1–449； UniProt 1–449 Author chain A7； PDBConstruct 1–449； UniProt 1–449 Author chain A9； PDBConstruct 1–449； UniProt 1–449 Author chain B1； PDBConstruct 1–449； UniProt 1–449 Author chain B3； PDBConstruct 1–449； UniProt 1–449 Author chain B5； PDBConstruct 1–449； UniProt 1–449 Author chain B7； PDBConstruct 1–449； UniProt 1–449 Author chain B9； PDBConstruct 1–449； UniProt 1–449 Author chain C1； PDBConstruct 1–449； UniProt 1–449 Author chain C3； PDBConstruct 1–449； UniProt 1–449 Author chain C5； PDBConstruct 1–449； UniProt 1–449 Author chain C7； PDBConstruct 1–449； UniProt 1–449 Author chain C9； PDBConstruct 1–449； UniProt 1–449 Author chain D1； PDBConstruct 1–449； UniProt 1–449 Author chain D3； PDBConstruct 1–449； UniProt 1–449 Author chain D5； PDBConstruct 1–449； UniProt 1–449 Author chain D7； PDBConstruct 1–449； UniProt 1–449 Author chain D9； PDBConstruct 1–449； UniProt 1–449 Author chain E1； PDBConstruct 1–449； UniProt 1–449 Author chain E3； PDBConstruct 1–449； UniProt 1–449 Author chain E5； PDBConstruct 1–449； UniProt 1–449 Author chain E7； PDBConstruct 1–449； UniProt 1–449 Author chain E9； PDBConstruct 1–449； UniProt 1–449 Author chain F1； PDBConstruct 1–449； UniProt 1–449

PDI family protein

OrganismNot specified

UniProt A0A125YMM3

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 × 100 PDB declaration: 100-meric（100） Consistent with protein copy count	Chain a； UniProt 1–220 Chain b； UniProt 1–220 Chain c； UniProt 1–220 Chain d； UniProt 1–220 Chain e； UniProt 1–220 Chain f； UniProt 1–220 Chain g； UniProt 1–220 Chain h； UniProt 1–220 Chain i； UniProt 1–220 Chain j； UniProt 1–220 Chain m； UniProt 1–220 Chain n； UniProt 1–220 Chain o； UniProt 1–220 Chain p； UniProt 1–220 Chain q； UniProt 1–220 Chain r； UniProt 1–220 Chain s； UniProt 1–220 Chain t； UniProt 1–220 Chain u； UniProt 1–220 Chain v； UniProt 1–220	Not recorded	Microtubule associated protein SPM1 × 24 （S8F1Y1） Tubulin alpha chain × 26 （P10873） Tubulin beta chain × 26 （A0A125YWG5） PDI family protein × 4 （A0A125YFI4）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.2；Phosphate Buffered Saline cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 8.40 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 7TNQ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7TNS Subpellicular microtubule from detergent-extract Toxoplasma gondii cells Deposited 2022-01-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 101 PDB declaration: 101-meric	Chain a 1–220（220 aa） Chain b 1–220（220 aa） Chain c 1–220（220 aa） Chain d 1–220（220 aa） Chain e 1–220（220 aa） Chain f 1–220（220 aa） Chain g 1–220（220 aa） Chain h 1–220（220 aa） Chain i 1–220（220 aa） Chain j 1–220（220 aa） Chain k 1–220（220 aa） Chain l 1–220（220 aa） Chain m 1–220（220 aa） Chain n 1–220（220 aa） Chain o 1–220（220 aa） Chain p 1–220（220 aa） Chain q 1–220（220 aa） Chain r 1–220（220 aa） Chain s 1–220（220 aa） Chain t 1–220（220 aa） Chain u 1–220（220 aa） Chain v 1–220（220 aa） Chain x 1–220（220 aa） Chain y 1–220（220 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Phosphate-Buffered Saline cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.70 Å

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

View Construct and Data Evidence

UniProt name	A0A125YMM3_TOXGM
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain a； PDBConstruct 1–220； UniProt 1–220 Author chain b； PDBConstruct 1–220； UniProt 1–220 Author chain c； PDBConstruct 1–220； UniProt 1–220 Author chain d； PDBConstruct 1–220； UniProt 1–220 Author chain e； PDBConstruct 1–220； UniProt 1–220 Author chain f； PDBConstruct 1–220； UniProt 1–220 Author chain g； PDBConstruct 1–220； UniProt 1–220 Author chain h； PDBConstruct 1–220； UniProt 1–220 Author chain i； PDBConstruct 1–220； UniProt 1–220 Author chain j； PDBConstruct 1–220； UniProt 1–220 Author chain m； PDBConstruct 1–220； UniProt 1–220 Author chain n； PDBConstruct 1–220； UniProt 1–220 Author chain o； PDBConstruct 1–220； UniProt 1–220 Author chain p； PDBConstruct 1–220； UniProt 1–220 Author chain q； PDBConstruct 1–220； UniProt 1–220 Author chain r； PDBConstruct 1–220； UniProt 1–220 Author chain s； PDBConstruct 1–220； UniProt 1–220 Author chain t； PDBConstruct 1–220； UniProt 1–220 Author chain u； PDBConstruct 1–220； UniProt 1–220 Author chain v； PDBConstruct 1–220； UniProt 1–220

PDI family protein

OrganismNot specified

UniProt A0A125YFI4

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 × 100 PDB declaration: 100-meric（100） Consistent with protein copy count	Chain k； UniProt 1–189 Chain l； UniProt 1–189 Chain w； UniProt 1–189 Chain x； UniProt 1–189	Not recorded	Microtubule associated protein SPM1 × 24 （S8F1Y1） Tubulin alpha chain × 26 （P10873） Tubulin beta chain × 26 （A0A125YWG5） PDI family protein × 20 （A0A125YMM3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.2；Phosphate Buffered Saline cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 8.40 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 7TNQ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7TNS Subpellicular microtubule from detergent-extract Toxoplasma gondii cells Deposited 2022-01-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 101 PDB declaration: 101-meric	Chain w 1–189（189 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Phosphate-Buffered Saline cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.70 Å

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

View Construct and Data Evidence

UniProt name	A0A125YFI4_TOXGM
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain k； PDBConstruct 1–189； UniProt 1–189 Author chain l； PDBConstruct 1–189； UniProt 1–189 Author chain w； PDBConstruct 1–189； UniProt 1–189 Author chain x； PDBConstruct 1–189； UniProt 1–189

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	7tnq
Deposition date deposition_date	2022-01-21
Structure title title	The symmetry-released subpellicular microtubule map from detergent-extracted Toxoplasma cells
Keywords keywords	parasites, Toxoplasma gondii, cytoskeleton, microtubules, tubulin, CELL INVASION; CELL INVASION
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	— Å
Radius of gyration Rg (electron density) rg_electron	121.50 Å
Forward intensity I(0) i0	128141000000.00
Molecular weight molecular_weight	3034700.0 kDa
Excluded volume excluded_volume	3779300 Å³
Envelope volume envelope_volume	6908000 Å³
Hydration-shell volume shell_volume	456500 Å³
Envelope diameter envelope_diameter	356.5 Å
Shell Rg shell_rg	137.70 Å
Envelope Rg envelope_rg	110.70 Å
Shape Rg shape_rg	121.50 Å
Total Rg total_rg	121.50 Å
Total atoms total_atoms	213168
Residues n_residues	27210
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	340.6 Å
Rg (real space) rg_real	122.00 Å
Rg uncertainty (real space) rg_real_error	1.25 Å
I(0) (real space) i0_real	1.2490e+11
I(0) uncertainty (real space) i0_real_error	2.8960e+09
Rg (reciprocal space) rg_reciprocal	128.30 Å
I(0) (reciprocal space) i0_reciprocal	130700000000.0000
Solution quality estimate total_estimate	0.8873
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	209.6 Å
Skewness Skewness skewness	-0.159
Kurtosis Kurtosis kurtosis	-0.757
Angular range angular_range	— – 0.0650 Å⁻¹
Current regularization parameter α current_alpha	1.7070
Highest regularization parameter α highest_alpha	3416000000.0000
Real-space data points n_real_points	14
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.928; Stabil: 0.931; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Microtubule associated protein SPM1
Molecular weight formula_weight	38817.7 kDa
Source method src_method	nat
Copy count entity_count	24

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	0,1,10,11,12,13,14,15,16,17,18,19,2,20,21,22,23,3,4,5,6,7,8,9
Atom count atom_count	213168

MSGGNSNTPKKLPSEEGSDYGYPQKPQKYLPKSEQAEPDYSACCKGNDAYKGASHGTVQFSHPEEAQKYAGAAAGAETIQRGRERVAADRQPRAAGDVPARRLHLSDVDEAHRGQSPSRHPGYCVEELCTCGMHKCIPSRAPVPFTGSTQYRQEFVPKPLPPPTQVSQVTLPPSLPFEAESSYRTEFVAKPLPPPAKFSEVKLPPTLPFHGESAYRTDYVPKPLPEVAKPVEVKLPPTLPFNAQSCYRSEYVAKPLPPPVQTAEVKLPPSLPFEGSTHYRDEFQVKPLPPATKVTEVKLPPSLPFDATSMYRSDYVAKSNPICPVSKLPQYPAATYPQNHVFWDPDTKQWY

Entity 2 Entity 2 polymer

Description description	Tubulin alpha chain
Molecular weight formula_weight	50166.6 kDa
Source method src_method	nat
Copy count entity_count	26

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A0,A2,A4,A6,A8,B0,B2,B4,B6,B8,C0,C2,C4,C6,C8,D0,D2,D4,D6,D8,E0,E2,E4,E6,E8,F0

MREVISIHVGQAGIQIGNACWELFCLEHGIQPDGQMPSDKTIGGGDDAFNTFFSETGAGKHVPRCVFLDLEPTVVDEVRTGTYRHLFHPEQLISGKEDAANNFARGHYTIGKEIVDLSLDRIRKLADNCTGLQGFLMFNAVGGGTGSGLGCLLLERLSVDYGKKSKLNFCSWPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDVTEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVMRAVCMISNSTAIAEVFSRMDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGIETAEGEGEEEGYGDEY

Entity 3 Entity 3 polymer

Description description	Tubulin beta chain
Molecular weight formula_weight	50119.1 kDa
Source method src_method	nat
Copy count entity_count	26

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A1,A3,A5,A7,A9,B1,B3,B5,B7,B9,C1,C3,C5,C7,C9,D1,D3,D5,D7,D9,E1,E3,E5,E7,E9,F1

MREIVHVQGGQCGNQIGAKFWEVISDEHGIDPTGTYCGDSDLQLERINVFYNEATGGRFVPRAILMDLEPGTMDSVRAGPFGQLFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPDRIMETFSVFPSPKVSDTVVEPYNATLSVHQLVENADEVQVIDNEALYDICFRTLKLTTPTYGDLNHLVSAAMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFLIGFAPLTSRGSQQYRALSVPELTQQMFDAKNMMCASDPRHGRYLTASAMFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNMKSSVCDIPPKGLKMSVTFVGNSTAIQEMFKRVSDQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEFDEEEGEMGAEEGA

Entity 4 Entity 4 polymer

Description description	PDI family protein
Molecular weight formula_weight	24939.3 kDa
EC 编号 ec_number	1.8.1.8
Source method src_method	nat
Copy count entity_count	20

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	a,b,c,d,e,f,g,h,i,j,m,n,o,p,q,r,s,t,u,v

MSQPVFASPLNVEKRRLNEERALMQAQKAGGEGVNIQLPPNYGDMDLILFPEGSLKNSNNTVIPQSHLKGKSVALYFADGADPKCASLLPFLLNYYRTMNEGGANQKIEIIFVSLDRDREAFESHRAHMPWLSIDLENPLTEILKRHFRVMKEYEVPTYGYGSRTGVPSVIVIGSDGREAQFLPICSGLEEGDRALLRWDWRNTKFASDQFHVRPTLLEQ

Entity 5 Entity 5 polymer

Description description	PDI family protein
Molecular weight formula_weight	21687.9 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	k,l,w,x

MLAADCFFGPDVVKRTQQGNYVPVRPDHFAGVSVALFFAKAGHSKCAQIVPVVRQFYKTTNFSGEKAVIEIIYVSLDKDEQDFERVRALMPWCSVEYKSCLRKKLIERYRVPNGELAFGTVRIPSTAIPLLIVIGPNGEEAGRMNFQQSDEFVLQRWDYRFNKWPGSAQRLRTLNDATDPWKKRLPQNV

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8. Citations (1)

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Resolution resolution	8.40 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	39122

fit	/app/data/saxs_computation/tn/7tnq/7tnq.fit
pddf	/app/data/pr_computation/tn/7tnq/7tnq.pr.out
profile	/app/data/saxs_computation/tn/7tnq/7tnq.dat

The symmetry-released subpellicular microtubule map from detergent-extracted Toxoplasma cells

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

Microtubule associated protein SPM1

State in the Current Structure

Other States of the Same Protein in the Database

Tubulin alpha chain

State in the Current Structure

Other States of the Same Protein in the Database

Tubulin beta chain

State in the Current Structure

Other States of the Same Protein in the Database

PDI family protein

State in the Current Structure

Other States of the Same Protein in the Database

PDI family protein

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)