9y9z

Cryo-EM structure of conoid fiber from Toxoplasma gondii (24-nm repeat)

Method: ELECTRON MICROSCOPY D_max: 529.1 Å Quality: EXCELLENT

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

CF2, TGME49_258090

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 × 378 PDB declaration: 378-meric（378） Consistent with protein copy count	Chain 1； UniProt 1–954 Chain 2； UniProt 1–954 Chain A； UniProt 1–954 Chain B； UniProt 1–954 Chain C； UniProt 1–954 Chain D； UniProt 1–954 Chain E； UniProt 1–954 Chain F； UniProt 1–954 Chain G； UniProt 1–954 Chain H； UniProt 1–954 Chain I； UniProt 1–954 Chain J； UniProt 1–954 Chain K； UniProt 1–954 Chain L； UniProt 1–954 Chain M； UniProt 1–954 Chain N； UniProt 1–954 Chain O； UniProt 1–954 Chain P； UniProt 1–954 Chain Q； UniProt 1–954 Chain R； UniProt 1–954 Chain S； UniProt 1–954 Chain T； UniProt 1–954 Chain U； UniProt 1–954 Chain V； UniProt 1–954 Chain W； UniProt 1–954 Chain X； UniProt 1–954 Chain Y； UniProt 1–954 Chain Z； UniProt 1–954 Chain a； UniProt 1–954 Chain b； UniProt 1–954 Chain c； UniProt 1–954 Chain d； UniProt 1–954 Chain e； UniProt 1–954 Chain f； UniProt 1–954 Chain g； UniProt 1–954 Chain h； UniProt 1–954 Chain i； UniProt 1–954 Chain j； UniProt 1–954 Chain k； UniProt 1–954 Chain l； UniProt 1–954 Chain m； UniProt 1–954 Chain n； UniProt 1–954 Chain o； UniProt 1–954 Chain p； UniProt 1–954 Chain q； UniProt 1–954 Chain r； UniProt 1–954 Chain s； UniProt 1–954 Chain t； UniProt 1–954 Chain u； UniProt 1–954 Chain v； UniProt 1–954 Chain w； UniProt 1–954 Chain x； UniProt 1–954 Chain y； UniProt 1–954 Chain z； UniProt 1–954	Not recorded	CF1, TGME49_222350 × 14 （S8GJP0） Tubulin alpha chain × 63 （P10873） Tubulin beta chain × 57 （I7BFC9） Spindle assembly abnormal protein 6 N-terminal domain-containing protein × 41 （A0A7J6KDX1） CIP3, TGME49_225020 × 7 （S8G5Q1） CF6, TGME49_245640 × 24 （A0A086KRX4） CF4, TGME49_246720 × 9 （A0A086KR31） CF3, TGME49_255895 × 7 （S8F3E8） CPH1, TGME49_266630 × 28 （A0A7J6KB56） Microtubule associated protein SPM1 × 5 （A0A7J6K285） PRP, TGME49_291880 × 35 （A0A151HK62） CF5, TGME49_297180 × 7 （S8FEB8） DCX, TGME49_256030 × 27 （B6KAS6） 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

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	S8GBZ2_TOXGM
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 1； PDBConstruct 1–954； UniProt 1–954 Author chain 2； PDBConstruct 1–954； UniProt 1–954 Author chain A； PDBConstruct 1–954； UniProt 1–954 Author chain B； PDBConstruct 1–954； UniProt 1–954 Author chain C； PDBConstruct 1–954； UniProt 1–954 Author chain D； PDBConstruct 1–954； UniProt 1–954 Author chain E； PDBConstruct 1–954； UniProt 1–954 Author chain F； PDBConstruct 1–954； UniProt 1–954 Author chain G； PDBConstruct 1–954； UniProt 1–954 Author chain H； PDBConstruct 1–954； UniProt 1–954 Author chain I； PDBConstruct 1–954； UniProt 1–954 Author chain J； PDBConstruct 1–954； UniProt 1–954 Author chain K； PDBConstruct 1–954； UniProt 1–954 Author chain L； PDBConstruct 1–954； UniProt 1–954 Author chain M； PDBConstruct 1–954； UniProt 1–954 Author chain N； PDBConstruct 1–954； UniProt 1–954 Author chain O； PDBConstruct 1–954； UniProt 1–954 Author chain P； PDBConstruct 1–954； UniProt 1–954 Author chain Q； PDBConstruct 1–954； UniProt 1–954 Author chain R； PDBConstruct 1–954； UniProt 1–954 Author chain S； PDBConstruct 1–954； UniProt 1–954 Author chain T； PDBConstruct 1–954； UniProt 1–954 Author chain U； PDBConstruct 1–954； UniProt 1–954 Author chain V； PDBConstruct 1–954； UniProt 1–954 Author chain W； PDBConstruct 1–954； UniProt 1–954 Author chain X； PDBConstruct 1–954； UniProt 1–954 Author chain Y； PDBConstruct 1–954； UniProt 1–954 Author chain Z； PDBConstruct 1–954； UniProt 1–954 Author chain a； PDBConstruct 1–954； UniProt 1–954 Author chain b； PDBConstruct 1–954； UniProt 1–954 Author chain c； PDBConstruct 1–954； UniProt 1–954 Author chain d； PDBConstruct 1–954； UniProt 1–954 Author chain e； PDBConstruct 1–954； UniProt 1–954 Author chain f； PDBConstruct 1–954； UniProt 1–954 Author chain g； PDBConstruct 1–954； UniProt 1–954 Author chain h； PDBConstruct 1–954； UniProt 1–954 Author chain i； PDBConstruct 1–954； UniProt 1–954 Author chain j； PDBConstruct 1–954； UniProt 1–954 Author chain k； PDBConstruct 1–954； UniProt 1–954 Author chain l； PDBConstruct 1–954； UniProt 1–954 Author chain m； PDBConstruct 1–954； UniProt 1–954 Author chain n； PDBConstruct 1–954； UniProt 1–954 Author chain o； PDBConstruct 1–954； UniProt 1–954 Author chain p； PDBConstruct 1–954； UniProt 1–954 Author chain q； PDBConstruct 1–954； UniProt 1–954 Author chain r； PDBConstruct 1–954； UniProt 1–954 Author chain s； PDBConstruct 1–954； UniProt 1–954 Author chain t； PDBConstruct 1–954； UniProt 1–954 Author chain u； PDBConstruct 1–954； UniProt 1–954 Author chain v； PDBConstruct 1–954； UniProt 1–954 Author chain w； PDBConstruct 1–954； UniProt 1–954 Author chain x； PDBConstruct 1–954； UniProt 1–954 Author chain y； PDBConstruct 1–954； UniProt 1–954 Author chain z； PDBConstruct 1–954； UniProt 1–954

CF1, TGME49_222350

OrganismNot specified

UniProt S8GJP0

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 × 378 PDB declaration: 378-meric（378） Consistent with protein copy count	Chain 10； UniProt 1–410 Chain 11； UniProt 1–410 Chain 12； UniProt 1–410 Chain 13； UniProt 1–410 Chain 14； UniProt 1–410 Chain 15； UniProt 1–410 Chain 16； UniProt 1–410 Chain 3； UniProt 1–410 Chain 4； UniProt 1–410 Chain 5； UniProt 1–410 Chain 6； UniProt 1–410 Chain 7； UniProt 1–410 Chain 8； UniProt 1–410 Chain 9； UniProt 1–410	Not recorded	CF2, TGME49_258090 × 54 （S8GBZ2） Tubulin alpha chain × 63 （P10873） Tubulin beta chain × 57 （I7BFC9） Spindle assembly abnormal protein 6 N-terminal domain-containing protein × 41 （A0A7J6KDX1） CIP3, TGME49_225020 × 7 （S8G5Q1） CF6, TGME49_245640 × 24 （A0A086KRX4） CF4, TGME49_246720 × 9 （A0A086KR31） CF3, TGME49_255895 × 7 （S8F3E8） CPH1, TGME49_266630 × 28 （A0A7J6KB56） Microtubule associated protein SPM1 × 5 （A0A7J6K285） PRP, TGME49_291880 × 35 （A0A151HK62） CF5, TGME49_297180 × 7 （S8FEB8） DCX, TGME49_256030 × 27 （B6KAS6） 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

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	S8GJP0_TOXGM
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain 10； PDBConstruct 1–410； UniProt 1–410 Author chain 11； PDBConstruct 1–410； UniProt 1–410 Author chain 12； PDBConstruct 1–410； UniProt 1–410 Author chain 13； PDBConstruct 1–410； UniProt 1–410 Author chain 14； PDBConstruct 1–410； UniProt 1–410 Author chain 15； PDBConstruct 1–410； UniProt 1–410 Author chain 16； PDBConstruct 1–410； UniProt 1–410 Author chain 3； PDBConstruct 1–410； UniProt 1–410 Author chain 4； PDBConstruct 1–410； UniProt 1–410 Author chain 5； PDBConstruct 1–410； UniProt 1–410 Author chain 6； PDBConstruct 1–410； UniProt 1–410 Author chain 7； PDBConstruct 1–410； UniProt 1–410 Author chain 8； PDBConstruct 1–410； UniProt 1–410 Author chain 9； PDBConstruct 1–410； UniProt 1–410

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 × 378 PDB declaration: 378-meric（378） Consistent with protein copy count	Chain 1A； UniProt 1–453 Chain 1C； UniProt 1–453 Chain 1E； UniProt 1–453 Chain 1G； UniProt 1–453 Chain 1I； UniProt 1–453 Chain 1K； UniProt 1–453 Chain 1M； UniProt 1–453 Chain 2A； UniProt 1–453 Chain 2C； UniProt 1–453 Chain 2E； UniProt 1–453 Chain 2G； UniProt 1–453 Chain 2I； UniProt 1–453 Chain 2K； UniProt 1–453 Chain 2M； UniProt 1–453 Chain 3A； UniProt 1–453 Chain 3C； UniProt 1–453 Chain 3E； UniProt 1–453 Chain 3G； UniProt 1–453 Chain 3I； UniProt 1–453 Chain 3K； UniProt 1–453 Chain 3M； UniProt 1–453 Chain 4A； UniProt 1–453 Chain 4C； UniProt 1–453 Chain 4E； UniProt 1–453 Chain 4G； UniProt 1–453 Chain 4I； UniProt 1–453 Chain 4K； UniProt 1–453 Chain 4M； UniProt 1–453 Chain 5A； UniProt 1–453 Chain 5C； UniProt 1–453 Chain 5E； UniProt 1–453 Chain 5G； UniProt 1–453 Chain 5I； UniProt 1–453 Chain 5K； UniProt 1–453 Chain 5M； UniProt 1–453 Chain 6A； UniProt 1–453 Chain 6C； UniProt 1–453 Chain 6E； UniProt 1–453 Chain 6G； UniProt 1–453 Chain 6I； UniProt 1–453 Chain 6K； UniProt 1–453 Chain 6M； UniProt 1–453 Chain 7A； UniProt 1–453 Chain 7C； UniProt 1–453 Chain 7E； UniProt 1–453 Chain 7G； UniProt 1–453 Chain 7I； UniProt 1–453 Chain 7K； UniProt 1–453 Chain 7M； UniProt 1–453 Chain 8A； UniProt 1–453 Chain 8C； UniProt 1–453 Chain 8E； UniProt 1–453 Chain 8G； UniProt 1–453 Chain 8I； UniProt 1–453 Chain 8K； UniProt 1–453 Chain 8M； UniProt 1–453 Chain 9A； UniProt 1–453 Chain 9C； UniProt 1–453 Chain 9E； UniProt 1–453 Chain 9G； UniProt 1–453 Chain 9I； UniProt 1–453 Chain 9K； UniProt 1–453 Chain 9M； UniProt 1–453	Not recorded	CF2, TGME49_258090 × 54 （S8GBZ2） CF1, TGME49_222350 × 14 （S8GJP0） Tubulin beta chain × 57 （I7BFC9） Spindle assembly abnormal protein 6 N-terminal domain-containing protein × 41 （A0A7J6KDX1） CIP3, TGME49_225020 × 7 （S8G5Q1） CF6, TGME49_245640 × 24 （A0A086KRX4） CF4, TGME49_246720 × 9 （A0A086KR31） CF3, TGME49_255895 × 7 （S8F3E8） CPH1, TGME49_266630 × 28 （A0A7J6KB56） Microtubule associated protein SPM1 × 5 （A0A7J6K285） PRP, TGME49_291880 × 35 （A0A151HK62） CF5, TGME49_297180 × 7 （S8FEB8） DCX, TGME49_256030 × 27 （B6KAS6） 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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9Y9Z	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 construct Different mutation/modification Different oligomeric state 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
7TNQ The symmetry-released subpellicular microtubule map from detergent-extracted Toxoplasma cells Deposited 2022-01-21	Different construct Different mutation/modification Different oligomeric state 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	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Phosphate Buffered Saline cryo-EM vitrification conditions Cryogen ETHANE	Resolution 8.40 Å
7TNS Subpellicular microtubule from detergent-extract Toxoplasma gondii cells Deposited 2022-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion 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 ligand/ion Different experimental conditions 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
9YA1 Cryo-EM structure of intraconoidal microtubule 2 (ICMT2) from Toxoplasma gondii (8-nm repeat) Deposited 2025-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion 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 construct Different mutation/modification Different oligomeric state Different ligand/ion 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 construct Different mutation/modification Different oligomeric state Different ligand/ion 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	3
Chains and sequence ranges	Author chain 1A； PDBConstruct 1–453； UniProt 1–453 Author chain 1C； PDBConstruct 1–453； UniProt 1–453 Author chain 1E； PDBConstruct 1–453； UniProt 1–453 Author chain 1G； PDBConstruct 1–453； UniProt 1–453 Author chain 1I； PDBConstruct 1–453； UniProt 1–453 Author chain 1K； PDBConstruct 1–453； UniProt 1–453 Author chain 1M； PDBConstruct 1–453； UniProt 1–453 Author chain 2A； PDBConstruct 1–453； UniProt 1–453 Author chain 2C； PDBConstruct 1–453； UniProt 1–453 Author chain 2E； PDBConstruct 1–453； UniProt 1–453 Author chain 2G； PDBConstruct 1–453； UniProt 1–453 Author chain 2I； PDBConstruct 1–453； UniProt 1–453 Author chain 2K； PDBConstruct 1–453； UniProt 1–453 Author chain 2M； PDBConstruct 1–453； UniProt 1–453 Author chain 3A； PDBConstruct 1–453； UniProt 1–453 Author chain 3C； PDBConstruct 1–453； UniProt 1–453 Author chain 3E； PDBConstruct 1–453； UniProt 1–453 Author chain 3G； PDBConstruct 1–453； UniProt 1–453 Author chain 3I； PDBConstruct 1–453； UniProt 1–453 Author chain 3K； PDBConstruct 1–453； UniProt 1–453 Author chain 3M； PDBConstruct 1–453； UniProt 1–453 Author chain 4A； PDBConstruct 1–453； UniProt 1–453 Author chain 4C； PDBConstruct 1–453； UniProt 1–453 Author chain 4E； PDBConstruct 1–453； UniProt 1–453 Author chain 4G； PDBConstruct 1–453； UniProt 1–453 Author chain 4I； PDBConstruct 1–453； UniProt 1–453 Author chain 4K； PDBConstruct 1–453； UniProt 1–453 Author chain 4M； PDBConstruct 1–453； UniProt 1–453 Author chain 5A； PDBConstruct 1–453； UniProt 1–453 Author chain 5C； PDBConstruct 1–453； UniProt 1–453 Author chain 5E； PDBConstruct 1–453； UniProt 1–453 Author chain 5G； PDBConstruct 1–453； UniProt 1–453 Author chain 5I； PDBConstruct 1–453； UniProt 1–453 Author chain 5K； PDBConstruct 1–453； UniProt 1–453 Author chain 5M； PDBConstruct 1–453； UniProt 1–453 Author chain 6A； PDBConstruct 1–453； UniProt 1–453 Author chain 6C； PDBConstruct 1–453； UniProt 1–453 Author chain 6E； PDBConstruct 1–453； UniProt 1–453 Author chain 6G； PDBConstruct 1–453； UniProt 1–453 Author chain 6I； PDBConstruct 1–453； UniProt 1–453 Author chain 6K； PDBConstruct 1–453； UniProt 1–453 Author chain 6M； PDBConstruct 1–453； UniProt 1–453 Author chain 7A； PDBConstruct 1–453； UniProt 1–453 Author chain 7C； PDBConstruct 1–453； UniProt 1–453 Author chain 7E； PDBConstruct 1–453； UniProt 1–453 Author chain 7G； PDBConstruct 1–453； UniProt 1–453 Author chain 7I； PDBConstruct 1–453； UniProt 1–453 Author chain 7K； PDBConstruct 1–453； UniProt 1–453 Author chain 7M； PDBConstruct 1–453； UniProt 1–453 Author chain 8A； PDBConstruct 1–453； UniProt 1–453 Author chain 8C； PDBConstruct 1–453； UniProt 1–453 Author chain 8E； PDBConstruct 1–453； UniProt 1–453 Author chain 8G； PDBConstruct 1–453； UniProt 1–453 Author chain 8I； PDBConstruct 1–453； UniProt 1–453 Author chain 8K； PDBConstruct 1–453； UniProt 1–453 Author chain 8M； PDBConstruct 1–453； UniProt 1–453 Author chain 9A； PDBConstruct 1–453； UniProt 1–453 Author chain 9C； PDBConstruct 1–453； UniProt 1–453 Author chain 9E； PDBConstruct 1–453； UniProt 1–453 Author chain 9G； PDBConstruct 1–453； UniProt 1–453 Author chain 9I； PDBConstruct 1–453； UniProt 1–453 Author chain 9K； PDBConstruct 1–453； UniProt 1–453 Author chain 9M； PDBConstruct 1–453； UniProt 1–453

Tubulin beta chain

OrganismNot specified

UniProt I7BFC9

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 × 378 PDB declaration: 378-meric（378） Consistent with protein copy count	Chain 1B； UniProt 1–449 Chain 1D； UniProt 1–449 Chain 1F； UniProt 1–449 Chain 1H； UniProt 1–449 Chain 1J； UniProt 1–449 Chain 1L； UniProt 1–449 Chain 1N； UniProt 1–449 Chain 2B； UniProt 1–449 Chain 2D； UniProt 1–449 Chain 2F； UniProt 1–449 Chain 2H； UniProt 1–449 Chain 2J； UniProt 1–449 Chain 2L； UniProt 1–449 Chain 3B； UniProt 1–449 Chain 3D； UniProt 1–449 Chain 3F； UniProt 1–449 Chain 3H； UniProt 1–449 Chain 3J； UniProt 1–449 Chain 3L； UniProt 1–449 Chain 4B； UniProt 1–449 Chain 4D； UniProt 1–449 Chain 4F； UniProt 1–449 Chain 4H； UniProt 1–449 Chain 4J； UniProt 1–449 Chain 4L； UniProt 1–449 Chain 5B； UniProt 1–449 Chain 5D； UniProt 1–449 Chain 5F； UniProt 1–449 Chain 5H； UniProt 1–449 Chain 5J； UniProt 1–449 Chain 5L； UniProt 1–449 Chain 5N； UniProt 1–449 Chain 6B； UniProt 1–449 Chain 6D； UniProt 1–449 Chain 6F； UniProt 1–449 Chain 6H； UniProt 1–449 Chain 6J； UniProt 1–449 Chain 6L； UniProt 1–449 Chain 6N； UniProt 1–449 Chain 7B； UniProt 1–449 Chain 7D； UniProt 1–449 Chain 7F； UniProt 1–449 Chain 7H； UniProt 1–449 Chain 7J； UniProt 1–449 Chain 7L； UniProt 1–449 Chain 8B； UniProt 1–449 Chain 8D； UniProt 1–449 Chain 8F； UniProt 1–449 Chain 8H； UniProt 1–449 Chain 8J； UniProt 1–449 Chain 8L； UniProt 1–449 Chain 9B； UniProt 1–449 Chain 9D； UniProt 1–449 Chain 9F； UniProt 1–449 Chain 9H； UniProt 1–449 Chain 9J； UniProt 1–449 Chain 9L； UniProt 1–449	Not recorded	CF2, TGME49_258090 × 54 （S8GBZ2） CF1, TGME49_222350 × 14 （S8GJP0） Tubulin alpha chain × 63 （P10873） Spindle assembly abnormal protein 6 N-terminal domain-containing protein × 41 （A0A7J6KDX1） CIP3, TGME49_225020 × 7 （S8G5Q1） CF6, TGME49_245640 × 24 （A0A086KRX4） CF4, TGME49_246720 × 9 （A0A086KR31） CF3, TGME49_255895 × 7 （S8F3E8） CPH1, TGME49_266630 × 28 （A0A7J6KB56） Microtubule associated protein SPM1 × 5 （A0A7J6K285） PRP, TGME49_291880 × 35 （A0A151HK62） CF5, TGME49_297180 × 7 （S8FEB8） DCX, TGME49_256030 × 27 （B6KAS6） 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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9Y9Z	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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 100 PDB declaration: 100-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	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
9YA1 Cryo-EM structure of intraconoidal microtubule 2 (ICMT2) from Toxoplasma gondii (8-nm repeat) Deposited 2025-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 96 PDB declaration: 96-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	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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 99 PDB declaration: 99-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	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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 108 PDB declaration: 108-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	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

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

View Construct and Data Evidence

UniProt name	I7BFC9_TOXGO
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain 1B； PDBConstruct 1–449； UniProt 1–449 Author chain 1D； PDBConstruct 1–449； UniProt 1–449 Author chain 1F； PDBConstruct 1–449； UniProt 1–449 Author chain 1H； PDBConstruct 1–449； UniProt 1–449 Author chain 1J； PDBConstruct 1–449； UniProt 1–449 Author chain 1L； PDBConstruct 1–449； UniProt 1–449 Author chain 1N； PDBConstruct 1–449； UniProt 1–449 Author chain 2B； PDBConstruct 1–449； UniProt 1–449 Author chain 2D； PDBConstruct 1–449； UniProt 1–449 Author chain 2F； PDBConstruct 1–449； UniProt 1–449 Author chain 2H； PDBConstruct 1–449； UniProt 1–449 Author chain 2J； PDBConstruct 1–449； UniProt 1–449 Author chain 2L； PDBConstruct 1–449； UniProt 1–449 Author chain 3B； PDBConstruct 1–449； UniProt 1–449 Author chain 3D； PDBConstruct 1–449； UniProt 1–449 Author chain 3F； PDBConstruct 1–449； UniProt 1–449 Author chain 3H； PDBConstruct 1–449； UniProt 1–449 Author chain 3J； PDBConstruct 1–449； UniProt 1–449 Author chain 3L； PDBConstruct 1–449； UniProt 1–449 Author chain 4B； PDBConstruct 1–449； UniProt 1–449 Author chain 4D； PDBConstruct 1–449； UniProt 1–449 Author chain 4F； PDBConstruct 1–449； UniProt 1–449 Author chain 4H； PDBConstruct 1–449； UniProt 1–449 Author chain 4J； PDBConstruct 1–449； UniProt 1–449 Author chain 4L； PDBConstruct 1–449； UniProt 1–449 Author chain 5B； PDBConstruct 1–449； UniProt 1–449 Author chain 5D； PDBConstruct 1–449； UniProt 1–449 Author chain 5F； PDBConstruct 1–449； UniProt 1–449 Author chain 5H； PDBConstruct 1–449； UniProt 1–449 Author chain 5J； PDBConstruct 1–449； UniProt 1–449 Author chain 5L； PDBConstruct 1–449； UniProt 1–449 Author chain 5N； PDBConstruct 1–449； UniProt 1–449 Author chain 6B； PDBConstruct 1–449； UniProt 1–449 Author chain 6D； PDBConstruct 1–449； UniProt 1–449 Author chain 6F； PDBConstruct 1–449； UniProt 1–449 Author chain 6H； PDBConstruct 1–449； UniProt 1–449 Author chain 6J； PDBConstruct 1–449； UniProt 1–449 Author chain 6L； PDBConstruct 1–449； UniProt 1–449 Author chain 6N； PDBConstruct 1–449； UniProt 1–449 Author chain 7B； PDBConstruct 1–449； UniProt 1–449 Author chain 7D； PDBConstruct 1–449； UniProt 1–449 Author chain 7F； PDBConstruct 1–449； UniProt 1–449 Author chain 7H； PDBConstruct 1–449； UniProt 1–449 Author chain 7J； PDBConstruct 1–449； UniProt 1–449 Author chain 7L； PDBConstruct 1–449； UniProt 1–449 Author chain 8B； PDBConstruct 1–449； UniProt 1–449 Author chain 8D； PDBConstruct 1–449； UniProt 1–449 Author chain 8F； PDBConstruct 1–449； UniProt 1–449 Author chain 8H； PDBConstruct 1–449； UniProt 1–449 Author chain 8J； PDBConstruct 1–449； UniProt 1–449 Author chain 8L； PDBConstruct 1–449； UniProt 1–449 Author chain 9B； PDBConstruct 1–449； UniProt 1–449 Author chain 9D； PDBConstruct 1–449； UniProt 1–449 Author chain 9F； PDBConstruct 1–449； UniProt 1–449 Author chain 9H； PDBConstruct 1–449； UniProt 1–449 Author chain 9J； PDBConstruct 1–449； UniProt 1–449 Author chain 9L； PDBConstruct 1–449； UniProt 1–449

Spindle assembly abnormal protein 6 N-terminal domain-containing protein

OrganismNot specified

UniProt A0A7J6KDX1

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 × 378 PDB declaration: 378-meric（378） Consistent with protein copy count	Chain 20； UniProt 1–263 Chain 21； UniProt 1–263 Chain 22； UniProt 1–263 Chain 23； UniProt 1–263 Chain 24； UniProt 1–263 Chain 25； UniProt 1–263 Chain 26； UniProt 1–263 Chain 27； UniProt 1–263 Chain 28； UniProt 1–263 Chain 29； UniProt 1–263 Chain 30； UniProt 1–263 Chain 31； UniProt 1–263 Chain 32； UniProt 1–263 Chain 33； UniProt 1–263 Chain 35； UniProt 1–263 Chain 36； UniProt 1–263 Chain 37； UniProt 1–263 Chain 38； UniProt 1–263 Chain 39； UniProt 1–263 Chain 40； UniProt 1–263 Chain 42； UniProt 1–263 Chain 43； UniProt 1–263 Chain 44； UniProt 1–263 Chain 45； UniProt 1–263 Chain 46； UniProt 1–263 Chain 47； UniProt 1–263 Chain 48； UniProt 1–263 Chain 49； UniProt 1–263 Chain 50； UniProt 1–263 Chain 51； UniProt 1–263 Chain 52； UniProt 1–263 Chain 53； UniProt 1–263 Chain 54； UniProt 1–263 Chain 55； UniProt 1–263 Chain 56； UniProt 1–263 Chain 57； UniProt 1–263 Chain 58； UniProt 1–263 Chain 59； UniProt 1–263 Chain 60； UniProt 1–263 Chain 61； UniProt 1–263 Chain 62； UniProt 1–263	Not recorded	CF2, TGME49_258090 × 54 （S8GBZ2） CF1, TGME49_222350 × 14 （S8GJP0） Tubulin alpha chain × 63 （P10873） Tubulin beta chain × 57 （I7BFC9） CIP3, TGME49_225020 × 7 （S8G5Q1） CF6, TGME49_245640 × 24 （A0A086KRX4） CF4, TGME49_246720 × 9 （A0A086KR31） CF3, TGME49_255895 × 7 （S8F3E8） CPH1, TGME49_266630 × 28 （A0A7J6KB56） Microtubule associated protein SPM1 × 5 （A0A7J6K285） PRP, TGME49_291880 × 35 （A0A151HK62） CF5, TGME49_297180 × 7 （S8FEB8） DCX, TGME49_256030 × 27 （B6KAS6） 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

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	A0A7J6KDX1_TOXGO
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain 20； PDBConstruct 1–263； UniProt 1–263 Author chain 21； PDBConstruct 1–263； UniProt 1–263 Author chain 22； PDBConstruct 1–263； UniProt 1–263 Author chain 23； PDBConstruct 1–263； UniProt 1–263 Author chain 24； PDBConstruct 1–263； UniProt 1–263 Author chain 25； PDBConstruct 1–263； UniProt 1–263 Author chain 26； PDBConstruct 1–263； UniProt 1–263 Author chain 27； PDBConstruct 1–263； UniProt 1–263 Author chain 28； PDBConstruct 1–263； UniProt 1–263 Author chain 29； PDBConstruct 1–263； UniProt 1–263 Author chain 30； PDBConstruct 1–263； UniProt 1–263 Author chain 31； PDBConstruct 1–263； UniProt 1–263 Author chain 32； PDBConstruct 1–263； UniProt 1–263 Author chain 33； PDBConstruct 1–263； UniProt 1–263 Author chain 35； PDBConstruct 1–263； UniProt 1–263 Author chain 36； PDBConstruct 1–263； UniProt 1–263 Author chain 37； PDBConstruct 1–263； UniProt 1–263 Author chain 38； PDBConstruct 1–263； UniProt 1–263 Author chain 39； PDBConstruct 1–263； UniProt 1–263 Author chain 40； PDBConstruct 1–263； UniProt 1–263 Author chain 42； PDBConstruct 1–263； UniProt 1–263 Author chain 43； PDBConstruct 1–263； UniProt 1–263 Author chain 44； PDBConstruct 1–263； UniProt 1–263 Author chain 45； PDBConstruct 1–263； UniProt 1–263 Author chain 46； PDBConstruct 1–263； UniProt 1–263 Author chain 47； PDBConstruct 1–263； UniProt 1–263 Author chain 48； PDBConstruct 1–263； UniProt 1–263 Author chain 49； PDBConstruct 1–263； UniProt 1–263 Author chain 50； PDBConstruct 1–263； UniProt 1–263 Author chain 51； PDBConstruct 1–263； UniProt 1–263 Author chain 52； PDBConstruct 1–263； UniProt 1–263 Author chain 53； PDBConstruct 1–263； UniProt 1–263 Author chain 54； PDBConstruct 1–263； UniProt 1–263 Author chain 55； PDBConstruct 1–263； UniProt 1–263 Author chain 56； PDBConstruct 1–263； UniProt 1–263 Author chain 57； PDBConstruct 1–263； UniProt 1–263 Author chain 58； PDBConstruct 1–263； UniProt 1–263 Author chain 59； PDBConstruct 1–263； UniProt 1–263 Author chain 60； PDBConstruct 1–263； UniProt 1–263 Author chain 61； PDBConstruct 1–263； UniProt 1–263 Author chain 62； PDBConstruct 1–263； UniProt 1–263

CIP3, TGME49_225020

OrganismNot specified

UniProt S8G5Q1

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 × 378 PDB declaration: 378-meric（378） Consistent with protein copy count	Chain 63； UniProt 1–1010 Chain 64； UniProt 1–1010 Chain 65； UniProt 1–1010 Chain 66； UniProt 1–1010 Chain 67； UniProt 1–1010 Chain 68； UniProt 1–1010 Chain 69； UniProt 1–1010	Not recorded	CF2, TGME49_258090 × 54 （S8GBZ2） CF1, TGME49_222350 × 14 （S8GJP0） Tubulin alpha chain × 63 （P10873） Tubulin beta chain × 57 （I7BFC9） Spindle assembly abnormal protein 6 N-terminal domain-containing protein × 41 （A0A7J6KDX1） CF6, TGME49_245640 × 24 （A0A086KRX4） CF4, TGME49_246720 × 9 （A0A086KR31） CF3, TGME49_255895 × 7 （S8F3E8） CPH1, TGME49_266630 × 28 （A0A7J6KB56） Microtubule associated protein SPM1 × 5 （A0A7J6K285） PRP, TGME49_291880 × 35 （A0A151HK62） CF5, TGME49_297180 × 7 （S8FEB8） DCX, TGME49_256030 × 27 （B6KAS6） 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

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	S8G5Q1_TOXGM
Isoform	—
PDB entities	6
Chains and sequence ranges	Author chain 63； PDBConstruct 1–1010； UniProt 1–1010 Author chain 64； PDBConstruct 1–1010； UniProt 1–1010 Author chain 65； PDBConstruct 1–1010； UniProt 1–1010 Author chain 66； PDBConstruct 1–1010； UniProt 1–1010 Author chain 67； PDBConstruct 1–1010； UniProt 1–1010 Author chain 68； PDBConstruct 1–1010； UniProt 1–1010 Author chain 69； PDBConstruct 1–1010； UniProt 1–1010

CF6, TGME49_245640

OrganismNot specified

UniProt A0A086KRX4

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 × 378 PDB declaration: 378-meric（378） Consistent with protein copy count	Chain 71； UniProt 1–416 Chain 72； UniProt 1–416 Chain 73； UniProt 1–416 Chain 75； UniProt 1–416 Chain 76； UniProt 1–416 Chain 77； UniProt 1–416 Chain 78； UniProt 1–416 Chain 79； UniProt 1–416 Chain 80； UniProt 1–416 Chain 82； UniProt 1–416 Chain 83； UniProt 1–416 Chain 84； UniProt 1–416 Chain 85； UniProt 1–416 Chain 86； UniProt 1–416 Chain 87； UniProt 1–416 Chain 89； UniProt 1–416 Chain 90； UniProt 1–416 Chain 91； UniProt 1–416 Chain 92； UniProt 1–416 Chain 93； UniProt 1–416 Chain 94； UniProt 1–416 Chain 95； UniProt 1–416 Chain 96； UniProt 1–416 Chain 97； UniProt 1–416	Not recorded	CF2, TGME49_258090 × 54 （S8GBZ2） CF1, TGME49_222350 × 14 （S8GJP0） Tubulin alpha chain × 63 （P10873） Tubulin beta chain × 57 （I7BFC9） Spindle assembly abnormal protein 6 N-terminal domain-containing protein × 41 （A0A7J6KDX1） CIP3, TGME49_225020 × 7 （S8G5Q1） CF4, TGME49_246720 × 9 （A0A086KR31） CF3, TGME49_255895 × 7 （S8F3E8） CPH1, TGME49_266630 × 28 （A0A7J6KB56） Microtubule associated protein SPM1 × 5 （A0A7J6K285） PRP, TGME49_291880 × 35 （A0A151HK62） CF5, TGME49_297180 × 7 （S8FEB8） DCX, TGME49_256030 × 27 （B6KAS6） 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

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	A0A086KRX4_TOXGO
Isoform	—
PDB entities	7
Chains and sequence ranges	Author chain 71； PDBConstruct 1–416； UniProt 1–416 Author chain 72； PDBConstruct 1–416； UniProt 1–416 Author chain 73； PDBConstruct 1–416； UniProt 1–416 Author chain 75； PDBConstruct 1–416； UniProt 1–416 Author chain 76； PDBConstruct 1–416； UniProt 1–416 Author chain 77； PDBConstruct 1–416； UniProt 1–416 Author chain 78； PDBConstruct 1–416； UniProt 1–416 Author chain 79； PDBConstruct 1–416； UniProt 1–416 Author chain 80； PDBConstruct 1–416； UniProt 1–416 Author chain 82； PDBConstruct 1–416； UniProt 1–416 Author chain 83； PDBConstruct 1–416； UniProt 1–416 Author chain 84； PDBConstruct 1–416； UniProt 1–416 Author chain 85； PDBConstruct 1–416； UniProt 1–416 Author chain 86； PDBConstruct 1–416； UniProt 1–416 Author chain 87； PDBConstruct 1–416； UniProt 1–416 Author chain 89； PDBConstruct 1–416； UniProt 1–416 Author chain 90； PDBConstruct 1–416； UniProt 1–416 Author chain 91； PDBConstruct 1–416； UniProt 1–416 Author chain 92； PDBConstruct 1–416； UniProt 1–416 Author chain 93； PDBConstruct 1–416； UniProt 1–416 Author chain 94； PDBConstruct 1–416； UniProt 1–416 Author chain 95； PDBConstruct 1–416； UniProt 1–416 Author chain 96； PDBConstruct 1–416； UniProt 1–416 Author chain 97； PDBConstruct 1–416； UniProt 1–416

CF4, TGME49_246720

OrganismNot specified

UniProt A0A086KR31

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 × 378 PDB declaration: 378-meric（378） Consistent with protein copy count	Chain A1； UniProt 1–502 Chain A2； UniProt 1–502 Chain A3； UniProt 1–502 Chain A4； UniProt 1–502 Chain A5； UniProt 1–502 Chain A6； UniProt 1–502 Chain A7； UniProt 1–502 Chain A8； UniProt 1–502 Chain A9； UniProt 1–502	Not recorded	CF2, TGME49_258090 × 54 （S8GBZ2） CF1, TGME49_222350 × 14 （S8GJP0） Tubulin alpha chain × 63 （P10873） Tubulin beta chain × 57 （I7BFC9） Spindle assembly abnormal protein 6 N-terminal domain-containing protein × 41 （A0A7J6KDX1） CIP3, TGME49_225020 × 7 （S8G5Q1） CF6, TGME49_245640 × 24 （A0A086KRX4） CF3, TGME49_255895 × 7 （S8F3E8） CPH1, TGME49_266630 × 28 （A0A7J6KB56） Microtubule associated protein SPM1 × 5 （A0A7J6K285） PRP, TGME49_291880 × 35 （A0A151HK62） CF5, TGME49_297180 × 7 （S8FEB8） DCX, TGME49_256030 × 27 （B6KAS6） 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

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	A0A086KR31_TOXGO
Isoform	—
PDB entities	8
Chains and sequence ranges	Author chain A1； PDBConstruct 1–502； UniProt 1–502 Author chain A2； PDBConstruct 1–502； UniProt 1–502 Author chain A3； PDBConstruct 1–502； UniProt 1–502 Author chain A4； PDBConstruct 1–502； UniProt 1–502 Author chain A5； PDBConstruct 1–502； UniProt 1–502 Author chain A6； PDBConstruct 1–502； UniProt 1–502 Author chain A7； PDBConstruct 1–502； UniProt 1–502 Author chain A8； PDBConstruct 1–502； UniProt 1–502 Author chain A9； PDBConstruct 1–502； UniProt 1–502

CF3, TGME49_255895

OrganismNot specified

UniProt S8F3E8

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 × 378 PDB declaration: 378-meric（378） Consistent with protein copy count	Chain B1； UniProt 1–556 Chain B2； UniProt 1–556 Chain B3； UniProt 1–556 Chain B4； UniProt 1–556 Chain B5； UniProt 1–556 Chain B6； UniProt 1–556 Chain B7； UniProt 1–556	Not recorded	CF2, TGME49_258090 × 54 （S8GBZ2） CF1, TGME49_222350 × 14 （S8GJP0） Tubulin alpha chain × 63 （P10873） Tubulin beta chain × 57 （I7BFC9） Spindle assembly abnormal protein 6 N-terminal domain-containing protein × 41 （A0A7J6KDX1） CIP3, TGME49_225020 × 7 （S8G5Q1） CF6, TGME49_245640 × 24 （A0A086KRX4） CF4, TGME49_246720 × 9 （A0A086KR31） CPH1, TGME49_266630 × 28 （A0A7J6KB56） Microtubule associated protein SPM1 × 5 （A0A7J6K285） PRP, TGME49_291880 × 35 （A0A151HK62） CF5, TGME49_297180 × 7 （S8FEB8） DCX, TGME49_256030 × 27 （B6KAS6） 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

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	S8F3E8_TOXGM
Isoform	—
PDB entities	9
Chains and sequence ranges	Author chain B1； PDBConstruct 1–556； UniProt 1–556 Author chain B2； PDBConstruct 1–556； UniProt 1–556 Author chain B3； PDBConstruct 1–556； UniProt 1–556 Author chain B4； PDBConstruct 1–556； UniProt 1–556 Author chain B5； PDBConstruct 1–556； UniProt 1–556 Author chain B6； PDBConstruct 1–556； UniProt 1–556 Author chain B7； PDBConstruct 1–556； UniProt 1–556

CPH1, TGME49_266630

OrganismNot specified

UniProt A0A7J6KB56

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 × 378 PDB declaration: 378-meric（378） Consistent with protein copy count	Chain C0； UniProt 1–582 Chain C6； UniProt 1–582 Chain C7； UniProt 1–582 Chain C8； UniProt 1–582 Chain C9； UniProt 1–582 Chain D0； UniProt 1–582 Chain D1； UniProt 1–582 Chain D2； UniProt 1–582 Chain D3； UniProt 1–582 Chain D4； UniProt 1–582 Chain D5； UniProt 1–582 Chain D6； UniProt 1–582 Chain D7； UniProt 1–582 Chain D8； UniProt 1–582 Chain D9； UniProt 1–582 Chain E0； UniProt 1–582 Chain E1； UniProt 1–582 Chain E2； UniProt 1–582 Chain E3； UniProt 1–582 Chain E4； UniProt 1–582 Chain E5； UniProt 1–582 Chain E6； UniProt 1–582 Chain E7； UniProt 1–582 Chain E8； UniProt 1–582 Chain E9； UniProt 1–582 Chain F1； UniProt 1–582 Chain F2； UniProt 1–582 Chain F3； UniProt 1–582	Not recorded	CF2, TGME49_258090 × 54 （S8GBZ2） CF1, TGME49_222350 × 14 （S8GJP0） Tubulin alpha chain × 63 （P10873） Tubulin beta chain × 57 （I7BFC9） Spindle assembly abnormal protein 6 N-terminal domain-containing protein × 41 （A0A7J6KDX1） CIP3, TGME49_225020 × 7 （S8G5Q1） CF6, TGME49_245640 × 24 （A0A086KRX4） CF4, TGME49_246720 × 9 （A0A086KR31） CF3, TGME49_255895 × 7 （S8F3E8） Microtubule associated protein SPM1 × 5 （A0A7J6K285） PRP, TGME49_291880 × 35 （A0A151HK62） CF5, TGME49_297180 × 7 （S8FEB8） DCX, TGME49_256030 × 27 （B6KAS6） 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

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	A0A7J6KB56_TOXGO
Isoform	—
PDB entities	10
Chains and sequence ranges	Author chain C0； PDBConstruct 1–582； UniProt 1–582 Author chain C6； PDBConstruct 1–582； UniProt 1–582 Author chain C7； PDBConstruct 1–582； UniProt 1–582 Author chain C8； PDBConstruct 1–582； UniProt 1–582 Author chain C9； PDBConstruct 1–582； UniProt 1–582 Author chain D0； PDBConstruct 1–582； UniProt 1–582 Author chain D1； PDBConstruct 1–582； UniProt 1–582 Author chain D2； PDBConstruct 1–582； UniProt 1–582 Author chain D3； PDBConstruct 1–582； UniProt 1–582 Author chain D4； PDBConstruct 1–582； UniProt 1–582 Author chain D5； PDBConstruct 1–582； UniProt 1–582 Author chain D6； PDBConstruct 1–582； UniProt 1–582 Author chain D7； PDBConstruct 1–582； UniProt 1–582 Author chain D8； PDBConstruct 1–582； UniProt 1–582 Author chain D9； PDBConstruct 1–582； UniProt 1–582 Author chain E0； PDBConstruct 1–582； UniProt 1–582 Author chain E1； PDBConstruct 1–582； UniProt 1–582 Author chain E2； PDBConstruct 1–582； UniProt 1–582 Author chain E3； PDBConstruct 1–582； UniProt 1–582 Author chain E4； PDBConstruct 1–582； UniProt 1–582 Author chain E5； PDBConstruct 1–582； UniProt 1–582 Author chain E6； PDBConstruct 1–582； UniProt 1–582 Author chain E7； PDBConstruct 1–582； UniProt 1–582 Author chain E8； PDBConstruct 1–582； UniProt 1–582 Author chain E9； PDBConstruct 1–582； UniProt 1–582 Author chain F1； PDBConstruct 1–582； UniProt 1–582 Author chain F2； PDBConstruct 1–582； UniProt 1–582 Author chain F3； PDBConstruct 1–582； UniProt 1–582

Microtubule associated protein SPM1

OrganismNot specified

UniProt A0A7J6K285

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 × 378 PDB declaration: 378-meric（378） Consistent with protein copy count	Chain C1； UniProt 1–351 Chain C2； UniProt 1–351 Chain C3； UniProt 1–351 Chain C4； UniProt 1–351 Chain C5； UniProt 1–351	Not recorded	CF2, TGME49_258090 × 54 （S8GBZ2） CF1, TGME49_222350 × 14 （S8GJP0） Tubulin alpha chain × 63 （P10873） Tubulin beta chain × 57 （I7BFC9） Spindle assembly abnormal protein 6 N-terminal domain-containing protein × 41 （A0A7J6KDX1） CIP3, TGME49_225020 × 7 （S8G5Q1） CF6, TGME49_245640 × 24 （A0A086KRX4） CF4, TGME49_246720 × 9 （A0A086KR31） CF3, TGME49_255895 × 7 （S8F3E8） CPH1, TGME49_266630 × 28 （A0A7J6KB56） PRP, TGME49_291880 × 35 （A0A151HK62） CF5, TGME49_297180 × 7 （S8FEB8） DCX, TGME49_256030 × 27 （B6KAS6） 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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9Y9Z	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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 100 PDB declaration: 100-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	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
9YA1 Cryo-EM structure of intraconoidal microtubule 2 (ICMT2) from Toxoplasma gondii (8-nm repeat) Deposited 2025-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 96 PDB declaration: 96-meric	Chain A 1–351（351 aa） Chain B 1–351（351 aa） Chain C 1–351（351 aa） Chain D 1–351（351 aa） Chain E 1–351（351 aa） Chain F 1–351（351 aa） Chain G 1–351（351 aa） Chain H 1–351（351 aa） Chain I 1–351（351 aa） Chain J 1–351（351 aa） Chain K 1–351（351 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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 99 PDB declaration: 99-meric	Chain A 1–351（351 aa） Chain B 1–351（351 aa） Chain C 1–351（351 aa） Chain D 1–351（351 aa） Chain E 1–351（351 aa） Chain F 1–351（351 aa） Chain G 1–351（351 aa） Chain H 1–351（351 aa） Chain I 1–351（351 aa） Chain J 1–351（351 aa） Chain K 1–351（351 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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 108 PDB declaration: 108-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 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	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

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

View Construct and Data Evidence

UniProt name	A0A7J6K285_TOXGO
Isoform	—
PDB entities	11
Chains and sequence ranges	Author chain C1； PDBConstruct 1–351； UniProt 1–351 Author chain C2； PDBConstruct 1–351； UniProt 1–351 Author chain C3； PDBConstruct 1–351； UniProt 1–351 Author chain C4； PDBConstruct 1–351； UniProt 1–351 Author chain C5； PDBConstruct 1–351； UniProt 1–351

PRP, TGME49_291880

OrganismNot specified

UniProt A0A151HK62

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 × 378 PDB declaration: 378-meric（378） Consistent with protein copy count	Chain F0； UniProt 1–783 Chain F5； UniProt 1–783 Chain F6； UniProt 1–783 Chain F7； UniProt 1–783 Chain F8； UniProt 1–783 Chain F9； UniProt 1–783 Chain G0； UniProt 1–783 Chain G1； UniProt 1–783 Chain G2； UniProt 1–783 Chain G3； UniProt 1–783 Chain G4； UniProt 1–783 Chain G5； UniProt 1–783 Chain G6； UniProt 1–783 Chain G7； UniProt 1–783 Chain G8； UniProt 1–783 Chain G9； UniProt 1–783 Chain H0； UniProt 1–783 Chain H1； UniProt 1–783 Chain H2； UniProt 1–783 Chain H3； UniProt 1–783 Chain H4； UniProt 1–783 Chain H5； UniProt 1–783 Chain H6； UniProt 1–783 Chain H7； UniProt 1–783 Chain H8； UniProt 1–783 Chain H9； UniProt 1–783 Chain I1； UniProt 1–783 Chain I2； UniProt 1–783 Chain I3； UniProt 1–783 Chain I4； UniProt 1–783 Chain I5； UniProt 1–783 Chain I6； UniProt 1–783 Chain I7； UniProt 1–783 Chain I8； UniProt 1–783 Chain I9； UniProt 1–783	Not recorded	CF2, TGME49_258090 × 54 （S8GBZ2） CF1, TGME49_222350 × 14 （S8GJP0） Tubulin alpha chain × 63 （P10873） Tubulin beta chain × 57 （I7BFC9） Spindle assembly abnormal protein 6 N-terminal domain-containing protein × 41 （A0A7J6KDX1） CIP3, TGME49_225020 × 7 （S8G5Q1） CF6, TGME49_245640 × 24 （A0A086KRX4） CF4, TGME49_246720 × 9 （A0A086KR31） CF3, TGME49_255895 × 7 （S8F3E8） CPH1, TGME49_266630 × 28 （A0A7J6KB56） Microtubule associated protein SPM1 × 5 （A0A7J6K285） CF5, TGME49_297180 × 7 （S8FEB8） DCX, TGME49_256030 × 27 （B6KAS6） 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

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	A0A151HK62_TOXGO
Isoform	—
PDB entities	12
Chains and sequence ranges	Author chain F0； PDBConstruct 1–783； UniProt 1–783 Author chain F5； PDBConstruct 1–783； UniProt 1–783 Author chain F6； PDBConstruct 1–783； UniProt 1–783 Author chain F7； PDBConstruct 1–783； UniProt 1–783 Author chain F8； PDBConstruct 1–783； UniProt 1–783 Author chain F9； PDBConstruct 1–783； UniProt 1–783 Author chain G0； PDBConstruct 1–783； UniProt 1–783 Author chain G1； PDBConstruct 1–783； UniProt 1–783 Author chain G2； PDBConstruct 1–783； UniProt 1–783 Author chain G3； PDBConstruct 1–783； UniProt 1–783 Author chain G4； PDBConstruct 1–783； UniProt 1–783 Author chain G5； PDBConstruct 1–783； UniProt 1–783 Author chain G6； PDBConstruct 1–783； UniProt 1–783 Author chain G7； PDBConstruct 1–783； UniProt 1–783 Author chain G8； PDBConstruct 1–783； UniProt 1–783 Author chain G9； PDBConstruct 1–783； UniProt 1–783 Author chain H0； PDBConstruct 1–783； UniProt 1–783 Author chain H1； PDBConstruct 1–783； UniProt 1–783 Author chain H2； PDBConstruct 1–783； UniProt 1–783 Author chain H3； PDBConstruct 1–783； UniProt 1–783 Author chain H4； PDBConstruct 1–783； UniProt 1–783 Author chain H5； PDBConstruct 1–783； UniProt 1–783 Author chain H6； PDBConstruct 1–783； UniProt 1–783 Author chain H7； PDBConstruct 1–783； UniProt 1–783 Author chain H8； PDBConstruct 1–783； UniProt 1–783 Author chain H9； PDBConstruct 1–783； UniProt 1–783 Author chain I1； PDBConstruct 1–783； UniProt 1–783 Author chain I2； PDBConstruct 1–783； UniProt 1–783 Author chain I3； PDBConstruct 1–783； UniProt 1–783 Author chain I4； PDBConstruct 1–783； UniProt 1–783 Author chain I5； PDBConstruct 1–783； UniProt 1–783 Author chain I6； PDBConstruct 1–783； UniProt 1–783 Author chain I7； PDBConstruct 1–783； UniProt 1–783 Author chain I8； PDBConstruct 1–783； UniProt 1–783 Author chain I9； PDBConstruct 1–783； UniProt 1–783

CF5, TGME49_297180

OrganismNot specified

UniProt S8FEB8

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 × 378 PDB declaration: 378-meric（378） Consistent with protein copy count	Chain J1； UniProt 1–871 Chain J2； UniProt 1–871 Chain J3； UniProt 1–871 Chain J4； UniProt 1–871 Chain J5； UniProt 1–871 Chain J6； UniProt 1–871 Chain J7； UniProt 1–871	Not recorded	CF2, TGME49_258090 × 54 （S8GBZ2） CF1, TGME49_222350 × 14 （S8GJP0） Tubulin alpha chain × 63 （P10873） Tubulin beta chain × 57 （I7BFC9） Spindle assembly abnormal protein 6 N-terminal domain-containing protein × 41 （A0A7J6KDX1） CIP3, TGME49_225020 × 7 （S8G5Q1） CF6, TGME49_245640 × 24 （A0A086KRX4） CF4, TGME49_246720 × 9 （A0A086KR31） CF3, TGME49_255895 × 7 （S8F3E8） CPH1, TGME49_266630 × 28 （A0A7J6KB56） Microtubule associated protein SPM1 × 5 （A0A7J6K285） PRP, TGME49_291880 × 35 （A0A151HK62） DCX, TGME49_256030 × 27 （B6KAS6） 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

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	S8FEB8_TOXGM
Isoform	—
PDB entities	13
Chains and sequence ranges	Author chain J1； PDBConstruct 1–871； UniProt 1–871 Author chain J2； PDBConstruct 1–871； UniProt 1–871 Author chain J3； PDBConstruct 1–871； UniProt 1–871 Author chain J4； PDBConstruct 1–871； UniProt 1–871 Author chain J5； PDBConstruct 1–871； UniProt 1–871 Author chain J6； PDBConstruct 1–871； UniProt 1–871 Author chain J7； PDBConstruct 1–871； UniProt 1–871

DCX, TGME49_256030

OrganismNot specified

UniProt B6KAS6

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 × 378 PDB declaration: 378-meric（378） Consistent with protein copy count	Chain K0； UniProt 1–256 Chain K1； UniProt 1–256 Chain K2； UniProt 1–256 Chain K3； UniProt 1–256 Chain K4； UniProt 1–256 Chain K5； UniProt 1–256 Chain K6； UniProt 1–256 Chain K7； UniProt 1–256 Chain K8； UniProt 1–256 Chain K9； UniProt 1–256 Chain L0； UniProt 1–256 Chain L1； UniProt 1–256 Chain L2； UniProt 1–256 Chain L3； UniProt 1–256 Chain L4； UniProt 1–256 Chain L5； UniProt 1–256 Chain L6； UniProt 1–256 Chain L7； UniProt 1–256 Chain L8； UniProt 1–256 Chain L9； UniProt 1–256 Chain M1； UniProt 1–256 Chain M2； UniProt 1–256 Chain M3； UniProt 1–256 Chain M4； UniProt 1–256 Chain M5； UniProt 1–256 Chain M6； UniProt 1–256 Chain M7； UniProt 1–256	Not recorded	CF2, TGME49_258090 × 54 （S8GBZ2） CF1, TGME49_222350 × 14 （S8GJP0） Tubulin alpha chain × 63 （P10873） Tubulin beta chain × 57 （I7BFC9） Spindle assembly abnormal protein 6 N-terminal domain-containing protein × 41 （A0A7J6KDX1） CIP3, TGME49_225020 × 7 （S8G5Q1） CF6, TGME49_245640 × 24 （A0A086KRX4） CF4, TGME49_246720 × 9 （A0A086KR31） CF3, TGME49_255895 × 7 （S8F3E8） CPH1, TGME49_266630 × 28 （A0A7J6KB56） Microtubule associated protein SPM1 × 5 （A0A7J6K285） PRP, TGME49_291880 × 35 （A0A151HK62） CF5, TGME49_297180 × 7 （S8FEB8） 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

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	DCXH_TOXGV
Isoform	—
PDB entities	14
Chains and sequence ranges	Author chain K0； PDBConstruct 1–256； UniProt 1–256 Author chain K1； PDBConstruct 1–256； UniProt 1–256 Author chain K2； PDBConstruct 1–256； UniProt 1–256 Author chain K3； PDBConstruct 1–256； UniProt 1–256 Author chain K4； PDBConstruct 1–256； UniProt 1–256 Author chain K5； PDBConstruct 1–256； UniProt 1–256 Author chain K6； PDBConstruct 1–256； UniProt 1–256 Author chain K7； PDBConstruct 1–256； UniProt 1–256 Author chain K8； PDBConstruct 1–256； UniProt 1–256 Author chain K9； PDBConstruct 1–256； UniProt 1–256 Author chain L0； PDBConstruct 1–256； UniProt 1–256 Author chain L1； PDBConstruct 1–256； UniProt 1–256 Author chain L2； PDBConstruct 1–256； UniProt 1–256 Author chain L3； PDBConstruct 1–256； UniProt 1–256 Author chain L4； PDBConstruct 1–256； UniProt 1–256 Author chain L5； PDBConstruct 1–256； UniProt 1–256 Author chain L6； PDBConstruct 1–256； UniProt 1–256 Author chain L7； PDBConstruct 1–256； UniProt 1–256 Author chain L8； PDBConstruct 1–256； UniProt 1–256 Author chain L9； PDBConstruct 1–256； UniProt 1–256 Author chain M1； PDBConstruct 1–256； UniProt 1–256 Author chain M2； PDBConstruct 1–256； UniProt 1–256 Author chain M3； PDBConstruct 1–256； UniProt 1–256 Author chain M4； PDBConstruct 1–256； UniProt 1–256 Author chain M5； PDBConstruct 1–256； UniProt 1–256 Author chain M6； PDBConstruct 1–256； UniProt 1–256 Author chain M7； PDBConstruct 1–256； UniProt 1–256

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9y9z
Deposition date deposition_date	2025-09-15
Structure title title	Cryo-EM structure of conoid fiber from Toxoplasma gondii (24-nm repeat)
Keywords keywords	;Tubulin, Microtubule, Microtubule Inner Protein, Microtubule-associated Protein, Toxoplasma gondii, conoid, conoid fiber, STRUCTURAL PROTEIN ;; STRUCTURAL PROTEIN
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	193.10 Å
Forward intensity I(0) i0	1870180000000.00
Molecular weight molecular_weight	11486000.0 kDa
Excluded volume excluded_volume	14269000 Å³
Envelope volume envelope_volume	26153000 Å³
Hydration-shell volume shell_volume	1111300 Å³
Envelope diameter envelope_diameter	669.3 Å
Shell Rg shell_rg	174.40 Å
Envelope Rg envelope_rg	191.30 Å
Shape Rg shape_rg	193.10 Å
Total Rg total_rg	193.00 Å
Total atoms total_atoms	806376
Residues n_residues	100974
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	529.1 Å
Rg (real space) rg_real	182.90 Å
Rg uncertainty (real space) rg_real_error	2.27 Å
I(0) (real space) i0_real	1.7530e+12
I(0) uncertainty (real space) i0_real_error	4.7530e+10
Rg (reciprocal space) rg_reciprocal	155.20 Å
I(0) (reciprocal space) i0_reciprocal	1584000000000.0000
Solution quality estimate total_estimate	0.9004
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	198.4 Å
Skewness Skewness skewness	0.346
Kurtosis Kurtosis kurtosis	-0.644
Angular range angular_range	— – 0.0400 Å⁻¹
Current regularization parameter α current_alpha	2.6090
Highest regularization parameter α highest_alpha	45390000000.0000
Real-space data points n_real_points	9
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.621; Oscil: 0.997; Stabil: 0.918; Sysdev: 1.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.001

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (17)

Entity 1 Entity 1 polymer

Description description	CF2, TGME49_258090
Molecular weight formula_weight	106251.1 kDa
Source method src_method	nat
Copy count entity_count	54

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,1,2,a,b,c,d,e,f,g,h,i,j,k,l,m,n,o,p,q,r,s,t,u,v,w,x,y,z
Atom count atom_count	806376

MATKQMLPGEGADRSSRPGTRSVARSRGTSPSSAPRLGISQELTALGSQLQALDRRQQLLFDPSVFPEDSRLAVSFPPFTRKVEDAAEAPHGAVKLRNPHRDGLDRVLGDLSKPVDLGVSLPAELQRDSFAQNDPPGRLPPALKHTSLRKLDEDAVSKFHVGVRQSARPVSYADALERTRREEDRQEKGAVRFAAATAAVAAAASAVGADADEIDCVVTVEEQAPPVCVSQGETNGGKSSGPGPGELRAEQAAAGSTVKMPADVYSAPGGAWRAAARAPSPEALAEPKVYSHSQWVDERRGEGGAPPGQFPFPRGLTEMQERMEEEWIDRERRLRADHKREMERAVAHASEKLSREYSRRLVFELQEQEKALLAQMHERHRQALAEIRCISESKTDAEEETQRFQREASAKEHQLQKVLHETRLIESEREALAAKVQHLEAENASLHASLTPLEKQACSQRAKEEDLQLRLERLKASNDRLQIQLQHEQQLAANFAQKRRGLEREVEVLDEKRAVAEREWKRVAAELRELQERQAGLCASNAHLQNELDNAIRHGRNLEQRIDEDRSKDDERQKLSQRLEKLQEEKETTERRQADEIASLRNRIKHLDAVTFQLRTMRQDFESQQLEVKRLRDENATLLAEMRHQNKGDHAMKLDQQALQNDLITVKQENADLRKEMNRLIKERNFAASGGSLPPYTPPRPNSFSTTPSPDNPLAMQLYSSEHSRGCGNACSGGGRQADPMMTEHDASVCPSLTGPLNRRCFTSDGRPRCVEDLSIPSPLSREACASPALRAQQLAVRCSTSINPVGRSTRPPPSVGAASNPLQHVHCPSAASRLGTEGDHPSYMYDGYRGDSRKATALGALAEDIPARGLAPAISLPVTAETPEQVASLESQLLLLATERRRIESELSKIPSARGRTARERQQMQHLESRLVEVDGTTHRIKQILFQAQRRKN

Entity 2 Entity 2 polymer

Description description	CF1, TGME49_222350
Molecular weight formula_weight	47976.3 kDa
Source method src_method	nat
Copy count entity_count	14

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	10,11,12,13,14,15,16,3,4,5,6,7,8,9

MQPLAREVSRLPRSGPLGPVAAKKDDKTFIPTNVRVSPGEKNDRVVKTEKIDDSTDGSGSHDGPRNLETQLEALTREVRELTLRVQEEKEMKELLNSQLNDAYEELADARSEHRVRGFAGASGARLRGVRGLPAFEARWMEPEHPTAQTAIRSQQEFELLLQEERARRHTMFEQYERHMKVMRKNHHKEKLETKKKVLSQVEFLIKKYRRLASDAVAVAKRERERVAEERKRARELAERACKNFEADLKGRTKTALEQYRRLVQEAHTAAKQEREELHNKCKELQETVDNERREFDTLIVREAEAKMAKFRASYARMKQQTEEERRQYGVMMHEIAKRVEKECAEYEEFVIRTMRDLLQSKGVEMTESGLRDFFQKKREEMRPSGEGHSSTDGLVTVKYRFQAADPEDLQ

Entity 3 Entity 3 polymer

Description description	Tubulin alpha chain
Molecular weight formula_weight	50166.6 kDa
Source method src_method	nat
Copy count entity_count	63

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	;1A,1C,1E,1G,1I,1K,1M,2A,2C,2E,2G,2I,2K,2M,3A,3C,3E,3G,3I,3K,3M,4A,4C,4E,4G,4I,4K,4M,5A,5C,5E,5G,5I,5K,5M,6A,6C,6E,6G,6I,6K,6M,7A,7C,7E,7G,7I,7K,7M,8A,8C,8E,8G,8I,8K,8M,9A,9C,9E,9G,9I,9K,9M ;

MREVISIHVGQAGIQIGNACWELFCLEHGIQPDGQMPSDKTIGGGDDAFNTFFSETGAGKHVPRCVFLDLEPTVVDEVRTGTYRHLFHPEQLISGKEDAANNFARGHYTIGKEIVDLSLDRIRKLADNCTGLQGFLMFNAVGGGTGSGLGCLLLERLSVDYGKKSKLNFCSWPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDVTEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVMRAVCMISNSTAIAEVFSRMDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGIETAEGEGEEEGYGDEY

Entity 4 Entity 4 polymer

Description description	Tubulin beta chain
Molecular weight formula_weight	50119.1 kDa
Source method src_method	nat
Copy count entity_count	57

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	;1B,1D,1F,1H,1J,1L,1N,2B,2D,2F,2H,2J,2L,3B,3D,3F,3H,3J,3L,4B,4D,4F,4H,4J,4L,5B,5D,5F,5H,5J,5L,5N,6B,6D,6F,6H,6J,6L,6N,7B,7D,7F,7H,7J,7L,8B,8D,8F,8H,8J,8L,9B,9D,9F,9H,9J,9L ;

MREIVHVQGGQCGNQIGAKFWEVISDEHGIDPTGTYCGDSDLQLERINVFYNEATGGRFVPRAILMDLEPGTMDSVRAGPFGQLFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPDRIMETFSVFPSPKVSDTVVEPYNATLSVHQLVENADEVQVIDNEALYDICFRTLKLTTPTYGDLNHLVSAAMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFLIGFAPLTSRGSQQYRALSVPELTQQMFDAKNMMCASDPRHGRYLTASAMFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNMKSSVCDIPPKGLKMSVTFVGNSTAIQEMFKRVSDQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEFDEEEGEMGAEEGA

Entity 5 Entity 5 polymer

Description description	Spindle assembly abnormal protein 6 N-terminal domain-containing protein
Molecular weight formula_weight	29530.0 kDa
Source method src_method	nat
Copy count entity_count	41

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	20,21,22,23,24,25,26,27,28,29,30,31,32,33,35,36,37,38,39,40,42,43,44,45,46,47,48,49,50,51,52,53,54,55,56,57,58,59,60,61,62

MATNFGFGGGASGCTDSVNFLAQVDTSAIDEMDPSLADGHTLVYSREVPFEIRLQETGSSLPGDVGRLEPIRVKILILGEETNPQHVRVELTSENDLFLNYTHALNEDLFRQMQERQKLMIEFGDYPSVLIKMLNSCIKEPHCFLAVLIMHTNGKARLDFIQSMEYKFIELLCLDCVQSTEEFTRRDMTFRYNALKSKLALLQARLHDIGCLLKLKSPSLLLHLQKAAQQQAHRRQQQVAAAAPIPGKLRAPGTTEGASTRFL

Entity 6 Entity 6 polymer

Description description	CIP3, TGME49_225020
Molecular weight formula_weight	114592.6 kDa
Source method src_method	nat
Copy count entity_count	7

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	63,64,65,66,67,68,69

MATQLGRSAPLSECEFLVASGRARAPGDPSRRSVSQPSRRNGSFREGLGPRSHDRELVGHPDIDKFRSTAGPQTSRARSARAAQPETLPRFYRPSSRMAAAKNETSRELRGKPPRPTSTLKYVGCPPTEPRLRPKRTSTGLEERMLKSGGYGVRIHWDEYAGYHVHASAPEVDLMHADQVLMVRDSPTHSRESDKDAAGSPPGGLSASLSPGRKATKKAGPVHCGVSRQCIPVYQFAPTLCEKSREIIDVYRKERVAHLWKKVDARREGVVDLFQLASRAPSRKTSKLRSSGMDAKSPDDTVLSSVEERFVQACVMQFVQIAVSRTSAQLVKDGATLGPHFDDSLRFTTAGAQGSENPPVVVPTEQAVFPHPHARDPMREGLQPDAEAEGAKIERENATAIQAAKRLARQHNQVIMLNVDANLGADASATPALFVPRKKFESVALEALAHEFGNPDIDVFRDRVMCECRKLVEKVNPEEAQRFFKPYILEYSRKLDARRRRAKAQEREESGRRAASLSADGYGPQGKFPTVGLRRVENRFDEQIEHYLRKKQQLHHLKEALDEMREGQFCTFHPAVNPYPKYLKQAFRLRRSPDDPLVILERFCEQYTEDREYPRLVEAIRECTFQPNIHKFVAKEKQLQATGVEVSQEKEKGITVPGKRIKEAHKQTTEDKPAAMESRVDHLFQSIERPFDHIFAADINQWLETDANLYSSQEDGAEKRKKQRWKRWEVEGRAPQYRGALKDRSQRALLTQDGGEVVVQLVEETEERAPVVLPRHRTTPYNDWVNGLRGGYLPNVMDFQKGPTEKGDRKKAERFNMRDWSRHIRLSEREVETRIIPNEEIIDAVCESELPSAAPPPPTIWVRRRRWEPAPERGPDAPTFTEAHFHTGSDRQTDRLLPAGKPAALTQQQAKEYKNRFASSVDPTTFVVPTPLKLDRLRQQYRLYMQLRNGIETGEIRTPPKVVTLRRDVLTDLEKEVKREPPTLVLAETRDAFASDTVETDNSVDGYVCE

Entity 7 Entity 7 polymer

Description description	CF6, TGME49_245640
Molecular weight formula_weight	46600.6 kDa
Source method src_method	nat
Copy count entity_count	24

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	71,72,73,75,76,77,78,79,80,82,83,84,85,86,87,89,90,91,92,93,94,95,96,97

MNQSTIVATSVVAPQSAVSLSRAPSRPGPSESFGKQQESRPGVSGAGLAESKRVPSLTQPSLERSVTISRRKIDAVGMSLVPKLDRTTTSLAAKEEKFSSIDKIVSKPTHSFGESSKLPAGIMKTKSMFPSQTLSAPWNAPARCARKDDFGTKAWIEKLQRETTDTSQPPLERQKSQRLAQTEPVQKLKTSWLEPPQEVESGHGVAEGDDLSVAAAEYHVPETEDGKLSFKPSDPRVWNREWIHRRIHNPVLSRSNRERCAFTQSNDWLVFALHHQYVRPLRSTDWLPGEACISQRDSFQLPPGAAKYTSSSLAIPQTSWEPFIFPNPPRPFLLRNKTFNSSARTWIPSRKVKAGLVGGGTEHACNLTQHEWLDLERMLWFDSEPRLEQPYRLYADSKTCIKGSVLDIGHMMRIGW

Entity 8 Entity 8 polymer

Description description	CF4, TGME49_246720
Molecular weight formula_weight	56022.8 kDa
Source method src_method	nat
Copy count entity_count	9

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A1,A2,A3,A4,A5,A6,A7,A8,A9

MVARVVEQDVARGSGRDTLARESDEAHPPQFSLSNPHFLTAVCEELKRRDKPVTGLTTAERFNAALADMGVRYGTPEADMIMRYCQVTEDGYVIFKELMLATRQLSNVSEDHVTESLSSATQREQDRLVPLPNTSARDRDSEQGEIRDERCVYTPELTDAIRRLYAQWDRSCLRDWQFKESLQRLGVCVTPEFERLLSTYGPSGCVSFSQVMQTLMMSDSGFLASSSLRRSRNRSAADIPLPPVADRLPFYEPRRNPVTWSPPQPLKGLPVNPQDVLQHALKLPLAADLDLDRRVGSEVGDTEGGDGCSLADKFRLLKKLVALYLSERLSATQFRKELVEADVPITPELDTLIRAHEADNSGQFTPFAVAVFRAAEETEIFLKEVRRASANTEAEAHSTRDTPYIVVDKLTQVDVPSTFPAQVEEEEDLKASARHMLEAGVKYPTEKEAFVGESKLGDIPKGNYIPSDYGMSQHATLALANRAAAHHAYHGHGNIITWGKSC

Entity 9 Entity 9 polymer

Description description	CF3, TGME49_255895
Molecular weight formula_weight	62988.6 kDa
Source method src_method	nat
Copy count entity_count	7

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B1,B2,B3,B4,B5,B6,B7

MTTASAIIGPSGGRDALMARQLYPNFFKTRAGDPPERGATRKDLRASMMDRKSILYPIPYLESEASRATWTQRATRGVPHLSTFSLAHAEPGGDIERDEIRETVASLLEVQPSGAQPLSVVYKRHDLEPLPPSISFRPHHNLADPVYYDMPPSPPYPAPPLLLKEQRRQKSLWSPLCNAESPEKRPHSIVFNPGCSFLSVTRGCRRGRRSNSAASEVSFQEVTGEPYHDLVQAESLRSRHRGREAAQLLSSRLGSLDEPQTNRHFPSPERRRKRAGATLGILPSRSVSVSAGSHRGRCRSSYPEESVPIPMPFWGRYDWYPPMKAPRQRIQAFGRPASRECVPLYESGLDDWTTFPWNETLRTTGHRSLTSEDRSPSTRFSPHRGSLRATGDNADLEWRMDRSTNFGELQSRIADASRGQQKFYRRQKASLWGALHPATQRVVGTFPRTECSFVCKEHRGRHVHLMDVFGPVERNRLSSYFDQDEADEIHRRARGCLGVHTASCPQSHNTLRKVLSDCAERGKPSDLDAFPQQTREPKRHWWSPAEPLADYADEKS

Entity 10 Entity 10 polymer

Description description	CPH1, TGME49_266630
Molecular weight formula_weight	67410.5 kDa
Source method src_method	nat
Copy count entity_count	28

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C0,C6,C7,C8,C9,D0,D1,D2,D3,D4,D5,D6,D7,D8,D9,E0,E1,E2,E3,E4,E5,E6,E7,E8,E9,F1,F2,F3

MSRAYADLVVSRKAKAPPFSVDNNDGRPKRPNRVWFDRDRAKACNDMRREYPLHYYISSYDVYAFLATLRQGADPAKRDAAGRTPLDLAVQMAVELIETSLCTSFPIDNIDVTPAATLKPAKDSPPESRPETFTNPFRVKYRDANASMYVQHDIMRYRCADSDVYKSCREPPFPLPSDGHDGAERTYQVATFPPQEFRIKNGDSEDFFRDQQRARRTQSPSFPLPRGDVSRYYAAAHNLRPQQFAYAYDANGKPMSWSRLQREQVQLEQEHLQGEFLVAVEQFLERPPSKAAMSQMRELIRRLNLMMVIIKKYELCLPLKREAAEKAKAYIGTALTYPYLYTASMYEAFKRYPRTPAGQAWDALNPADSRRLVLIILSLKMHGHELFSFMGTVCRLFNSLMEQLGLCDDRCGTGGHWCKLGSECSQFYLHMAFSLDDAQLFQKFITQQQLFDKQDIFKWEDLLYTLMQHRERFRPYFAALLARRLKARVQKRLMNSADQQAYLPETVKYPCEERYFTRQLLGEYSEIFGESEAEEFNSMLRHWRYGAARQAPGTGSEEDNILPAPLPPVSESPAADFWSLRD

Entity 11 Entity 11 polymer

Description description	Microtubule associated protein SPM1
Molecular weight formula_weight	38845.8 kDa
Source method src_method	nat
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C1,C2,C3,C4,C5

MSGGNSNTPKKLPSEEGSDYGYPQKPQKYLPKSEQAEPDYSACCKGNDAYKGASHGTVQFSHPEEAQKYAGAAAGAETIQRGRERVAADRQPRAAGDVPARRLHLSDVDEAHRGQSPSRHPGYCVEELCTCGMHKCIPSRAPVPFTGSTQYRQEFVPKPLPPPTQVSQVTLPPSLPFEAESSYRTEFVAKPLPPPAKFSEVKLPPTLPFHGESAYRTDYVPKPLPEVAKPVEVKLPPTLPFNAQSCYRSEYVAKPLPPPVQTVEVKLPPSLPFEGSTHYRDEFQVKPLPPATKVTEVKLPPSLPFDATSMYRSDYVAKSNPICPVSKLPQYPAATYPQNHVFWDPDTKQWY

Entity 12 Entity 12 polymer

Description description	PRP, TGME49_291880
Molecular weight formula_weight	80452.4 kDa
Source method src_method	nat
Copy count entity_count	35

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F0,F5,F6,F7,F8,F9,G0,G1,G2,G3,G4,G5,G6,G7,G8,G9,H0,H1,H2,H3,H4,H5,H6,H7,H8,H9,I1,I2,I3,I4,I5,I6,I7,I8,I9

MLARGDDELCSSFYRSANKHIRGVGGEPPASSRADLRRYMPGYTAPPSLNAYKAWHVNSATLRRENDRLKAENKNIERDFDRLYQRAYIAEVQLNNLKAAASKIPLGGANYSVTQLVKLAANLLELLTKQPEQTCVSVIPDALACLSMCHVRDRRLFAAGEKLKRTLQCPSGASGYNGNESKTRPIGRPAGEVAPDLKWLATVSDDLSWLKWADQWDVLPMDLRWISIAVDDRSLLLHRFLWTRAPVDLRYLTVVSGNMDWLYIGPDRWYSTPMQLRLRAIALEDPTIIKPTMAEAALYGLEREKIANTLIPDADLPNLPSPHAPEEDLDLTLRISLSPADIAVCENNGGIASSAKAGASTGTPGMPTPGSKVGQAKETSASSKVGMAKTVPSPLSKTAPPLKADPSEPVPTKVGGGSVGGPKATPSPSKAGPPPKDSDKPGGVAKKASPTPPSKAEGVAASGSGDAPEEPKSVKGAPLGKKGPGPLGVKGGSPLPPPGDAKGKASPESATAKGPAELPKGPAGAAKAAVPGKAAPVGPGKGPAAPLGKKAPGEPVGKPKAEMKKSSPPVGEPKAEVKKSPPPPSGSPKAESKKSPSPPLGEPKADVKKSPPPPLGGPKAEMKKSPPGASPAAPKADSSTPAAPTGATPPKAKLGAPPGKAPTAGTAEGKEAAPAKKGPLPAKGAEPLGKKGPPPVAKAEDTTKPPPPTAGQNDDADGAGVSAKKQSPLGKGPPPKKGPLLGKKIPPAPDARDAKADDASPAKKGPPKGLPKGKAPPKGKGFL

Entity 13 Entity 13 polymer

Description description	CF5, TGME49_297180
Molecular weight formula_weight	97829.7 kDa
Source method src_method	nat
Copy count entity_count	7

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J1,J2,J3,J4,J5,J6,J7

MSRERLGPSRLGRHTPAAASARGDPRLLVEAETPTDRGRIVKASLHTQGDVEFLEGRLRDKVCVDKWVTVQERASPAEGKRESEGKRESEGRRESPRMTSTSAGLEPAEAWREDIFGKEERYDMARFDEEDASAEDAVRTAPRPSPQRQFQVRHKVTVEGVVPTSASVRMQRRLAQRRGKRFFSTDEGLYWQKLQRSKPQKSREDALKFVATFMQEGELLVNSVSMEEDPSVRLRRLAALRLLRNSPADRVPGSISGRLLIPYDHADVRELLRVSSFCSGEAWRVLEEIRRLLVLRKGRLFLASDRNATASRHCLAFLASLKKNLEAAARNLVRQGRLRRPSARLQQSEGRKRAPTLDRDEAWERREGLVREIRRTLSLAAAYSTKGKKQPVVYIQLAALKPSIVADFLTPAEVAVILTEVFQNLWTKFVEYSLRRRVRVSTAALVLDFSGLTEFELASSASHFLLSSLRDVVRAFAPLLIKKIIFYNSAKAGEFLWEALRPGVEHSCFFSFCSSEEDLETEIESERTMVYHTTGLANDMSLIAHRCPLYALYGPPLPPPDSLFPLRAPGFLPASAPASALQKSPLSRPKAGAFRQLFALLGAARVRLVPTAEDAETGGSNLPRAPFFRTAGESRERENAGLARGGEEDEETETLRRGDEEIQKTCREEEAKFWRGMNCFHDLVVEAARAKRIAERERQADVVESARQTRPAEAKPDEADEDAEELDLDSVDVIDPDANLGPSEESLECAAAAVAQDGDRVDLGKSHAERSFERIFTAQGDLEETLEGIGSPFENAWERSVQEAFDASVKAIREEHLPLSAARVELPRVSRPARTFPTPLDRVFRRPLYLHLSAEAGGNWERELLGADRAK

Entity 14 Entity 14 polymer

Description description	DCX, TGME49_256030
Molecular weight formula_weight	29261.4 kDa
Source method src_method	nat
Copy count entity_count	27

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	K0,K1,K2,K3,K4,K5,K6,K7,K8,K9,L0,L1,L2,L3,L4,L5,L6,L7,L8,L9,M1,M2,M3,M4,M5,M6,M7

MACGIPWKLARRDELMATRQAERPGEYFPPPYPPCPPTVVTPLRTSAYDFPEATFVTRPCLPAKKATGHKNVFERLTDTAYYTGSHRERFDEFGNGRGIAGREYLYAYDGLTESPSRCHEVYSSVIKRPRKPVVTPGTLGIQRFGVQIPAPRLMWLYRNGDKHDDGTPFFVRPYIKSMESLYQQITKEITPIAGPVRRIFDQNFRVITDLDDIVDGAKYLCTSGEPPAAYDRLEKFLSEWVIQKSQTKVPSQFFVV

Entity 15 Entity 15 non-polymer

Description description	GUANOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	523.2 kDa
Source method src_method	syn
Copy count entity_count	63

Entity 16 Entity 16 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	54

Entity 17 Entity 17 non-polymer

Description description	GUANOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	443.2 kDa
Source method src_method	syn
Copy count entity_count	57

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8. Citations (1)

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Resolution resolution	3.14 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	95409

fit	/app/data/saxs_computation/y9/9y9z/9y9z.fit
pddf	/app/data/pr_computation/y9/9y9z/9y9z.pr.out
profile	/app/data/saxs_computation/y9/9y9z/9y9z.dat

Cryo-EM structure of conoid fiber from Toxoplasma gondii (24-nm repeat)

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

CF2, TGME49_258090

State in the Current Structure

Other States of the Same Protein in the Database

CF1, TGME49_222350

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

Spindle assembly abnormal protein 6 N-terminal domain-containing protein

State in the Current Structure

Other States of the Same Protein in the Database

CIP3, TGME49_225020

State in the Current Structure

Other States of the Same Protein in the Database

CF6, TGME49_245640

State in the Current Structure

Other States of the Same Protein in the Database

CF4, TGME49_246720

State in the Current Structure

Other States of the Same Protein in the Database

CF3, TGME49_255895

State in the Current Structure

Other States of the Same Protein in the Database

CPH1, TGME49_266630

State in the Current Structure

Other States of the Same Protein in the Database

Microtubule associated protein SPM1

State in the Current Structure

Other States of the Same Protein in the Database

PRP, TGME49_291880

State in the Current Structure

Other States of the Same Protein in the Database

CF5, TGME49_297180

State in the Current Structure

Other States of the Same Protein in the Database

DCX, TGME49_256030

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 (17)

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 polymer

Polymer Polymer

Entity 8 Entity 8 polymer

Polymer Polymer

Entity 9 Entity 9 polymer

Polymer Polymer

Entity 10 Entity 10 polymer

Polymer Polymer

Entity 11 Entity 11 polymer

Polymer Polymer

Entity 12 Entity 12 polymer

Polymer Polymer

Entity 13 Entity 13 polymer

Polymer Polymer

Entity 14 Entity 14 polymer

Polymer Polymer