5jco

Structure and dynamics of single-isoform recombinant neuronal human tubulin

Method: ELECTRON MICROSCOPY D_max: 228.2 Å Quality: GOOD

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

Tubulin beta-3 chain

Homo sapiens

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 × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain C； UniProt 1–426 Chain D； UniProt 1–426 Chain I； UniProt 1–426 Chain J； UniProt 1–426 Chain K； UniProt 1–426 Chain L； UniProt 1–426	Not recorded	Tubulin alpha-1A chain × 6 （Q71U36） G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 6 MG MAGNESIUM ION × 12 GTP GUANOSINE-5'-TRIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer：pH 6.9 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.00 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 5JCO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
22AJ GDP human alpha1A/beta3 S239C microtubule Deposited 2026-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–450（450 aa）	Mutation：S239C	MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.48 Å
22AK GDP human alpha1A/beta3 microtubule Deposited 2026-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–450（450 aa）	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.41 Å
5IJ0 Cryo EM density of microtubule assembled from human TUBB3 Deposited 2016-03-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–426（426 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
5IJ9 Cryo EM density of microtubule assembled from human TUBB3-D417H mutant Deposited 2016-03-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–426（426 aa）	Mutation：D417H	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
6E7B 13-pf 3-start GMPCPP-human alpha1B/beta3 microtubules Deposited 2018-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–426（426 aa）	Not recorded	MG MAGNESIUM ION × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
6S8L Structure, Thermodynamics, and Kinetics of Plinabulin Binding to two Tubulin Isotypes Deposited 2019-07-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–450（450 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 PN6 (3Z,6Z)-3-benzylidene-6-[(5-tert-butyl-1H-imidazol-4-yl)methylidene]piperazine-2,5-dione × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；100 mM Bis-TrisMethane, pH 5.5, supplemented with 200 mM ammonium sulfate and 25% PEG3350	Resolution 1.80 Å R-free 0.266
6WSL Cryo-EM structure of VASH1-SVBP bound to microtubules Deposited 2020-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 1–450（450 aa） Chain F 1–450（450 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
7LXB HeLa-tubulin in complex with cryptophycin 52 Deposited 2021-03-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain B 1–450（450 aa） Chain D 1–450（450 aa） Chain F 1–450（450 aa） Chain H 1–450（450 aa） Chain J 1–450（450 aa） Chain L 1–450（450 aa） Chain N 1–450（450 aa） Chain P 1–450（450 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 8 YGY Cryptophycin 52 × 8 GDP GUANOSINE-5'-DIPHOSPHATE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 6.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.26 Å
7M18 HeLa-tubulin in complex with cryptophycin 1 Deposited 2021-03-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain B 1–450（450 aa） Chain D 1–450（450 aa） Chain F 1–450（450 aa） Chain H 1–450（450 aa） Chain J 1–450（450 aa） Chain L 1–450（450 aa） Chain N 1–450（450 aa） Chain P 1–450（450 aa）	Not recorded	YNP Cryptophycin 1 × 8 GDP GUANOSINE-5'-DIPHOSPHATE × 8 GTP GUANOSINE-5'-TRIPHOSPHATE × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 6.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.38 Å
7M20 18-mer HeLa-tubulin rings in complex with Cryptophycin 1 Deposited 2021-03-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain B 1–450（450 aa） Chain D 1–450（450 aa） Chain F 1–450（450 aa） Chain H 1–450（450 aa） Chain J 1–450（450 aa） Chain L 1–450（450 aa） Chain N 1–450（450 aa） Chain P 1–450（450 aa） Chain R 1–450（450 aa）	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 9 YNP Cryptophycin 1 × 9 GTP GUANOSINE-5'-TRIPHOSPHATE × 9	ELECTRON MICROSCOPY cryo-EM buffer pH 6.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.84 Å
7PJF Inhibiting parasite proliferation using a rationally designed anti-tubulin agent Deposited 2021-08-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–450（450 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；293 K；100 mM Bis-TrisMethane, pH 5.5, supplemented with 200 mM ammonium sulfate and 25% PEG3350	Resolution 1.86 Å R-free 0.218
7SJ7 Undecorated 13pf wildtype microtubule from recombinant human tubulin Deposited 2021-10-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain B 1–450（450 aa） Chain D 1–450（450 aa） Chain F 1–450（450 aa） Chain G 1–450（450 aa） Chain H 1–450（450 aa） Chain I 1–450（450 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 6 GDP GUANOSINE-5'-DIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8；80 mM PIPES, 1 mM EGTA, 5 mM MgCl2, 2 mM GTP, pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.80 Å
7SJ8 13pf wildtype microtubule from recombinant human tubulin decorated with kinesin Deposited 2021-10-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain B 1–450（450 aa） Chain D 1–450（450 aa） Chain F 1–450（450 aa） Chain G 1–450（450 aa） Chain H 1–450（450 aa） Chain I 1–450（450 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 6 GDP GUANOSINE-5'-DIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8；80 mM PIPES, 1 mM EGTA, 5 mM MgCl2, 2 mM GTP, pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；30 second adsorption time onto grid. blot force 15, 4 second blot time, 37 degrees, and 100 percent humidity. 0.5 second drain time.	Resolution 3.60 Å
7SJ9 13pf E254A microtubule from recombinant human tubulin decorated with EB3 Deposited 2021-10-16	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain B 1–450（450 aa） Chain D 1–450（450 aa） Chain F 1–450（450 aa） Chain G 1–450（450 aa） Chain H 1–450（450 aa） Chain I 1–450（450 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8；80 mM PIPES, 1 mM EGTA, 5 mM MgCl2, 2 mM GTP, pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.80 Å
7SJA Undecorated 13pf E254N microtubule from recombinant human tubulin Deposited 2021-10-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain B 1–450（450 aa） Chain D 1–450（450 aa） Chain F 1–450（450 aa） Chain G 1–450（450 aa） Chain H 1–450（450 aa） Chain I 1–450（450 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8；80 mM PIPES, 1 mM EGTA, 5 mM MgCl2, 2 mM GTP, pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.80 Å
7Z6S MATCAP bound to a human 14 protofilament microtubule Deposited 2022-03-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: Hexameric	Chain B 1–450（450 aa） Chain H 1–450（450 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
8VRJ Rigid body fitted model for gamma tubulin ring complex capped microtubule Deposited 2024-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 60 PDB declaration: 60-meric	Chain 2 1–450（450 aa） Chain o 1–450（450 aa） Chain p 1–450（450 aa） Chain q 1–450（450 aa） Chain r 1–450（450 aa） Chain s 1–450（450 aa） Chain t 1–450（450 aa） Chain u 1–450（450 aa） Chain v 1–450（450 aa） Chain w 1–450（450 aa） Chain x 1–450（450 aa） Chain y 1–450（450 aa） Chain z 1–450（450 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.70 Å
8VRK Rigid body fitted model for refined density map of gamma tubulin ring complex capped microtubule Deposited 2024-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 60 PDB declaration: 60-meric	Chain 2 1–450（450 aa） Chain o 1–450（450 aa） Chain p 1–450（450 aa） Chain q 1–450（450 aa） Chain r 1–450（450 aa） Chain s 1–450（450 aa） Chain t 1–450（450 aa） Chain u 1–450（450 aa） Chain v 1–450（450 aa） Chain w 1–450（450 aa） Chain x 1–450（450 aa） Chain y 1–450（450 aa） Chain z 1–450（450 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 8.50 Å
8VT7 Structure of the gamma tubulin ring complex nucleated microtubule protofilament. Deposited 2024-01-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–450（450 aa） Chain F 1–450（450 aa）	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.66 Å
9F3B Undecorated 13pf E254Q microtubule from recombinant human tubulin Deposited 2024-04-25	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric	Chain B 1–450（450 aa） Chain D 1–450（450 aa） Chain F 1–450（450 aa） Chain N 1–450（450 aa） Chain P 1–450（450 aa） Chain R 1–450（450 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
9F3H Undecorated 13pf mosaic 20%E254Q - 80% E254QN microtubule from recombinant human tubulin Deposited 2024-04-25	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric	Chain B 1–450（450 aa） Chain D 1–450（450 aa） Chain F 1–450（450 aa） Chain N 1–450（450 aa） Chain P 1–450（450 aa） Chain R 1–450（450 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.30 Å
9F3R 13pf E254Q microtubule from recombinant human tubulin decorated with EB3 Deposited 2024-04-25	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: 14-meric	Chain B 1–450（450 aa） Chain D 1–450（450 aa） Chain F 1–450（450 aa） Chain N 1–450（450 aa） Chain P 1–450（450 aa） Chain R 1–450（450 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.30 Å
9F3S 13pf mosaic 20%E254Q - 80% E254N microtubule from recombinant human tubulin decorated with EB3 Deposited 2024-04-25	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: 14-meric	Chain B 1–450（450 aa） Chain D 1–450（450 aa） Chain F 1–450（450 aa） Chain N 1–450（450 aa） Chain P 1–450（450 aa） Chain R 1–450（450 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.20 Å
9SMX CM1-activated gTuRC in complex with nascent alpha-E254D mutant microtubules Deposited 2025-09-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 73 PDB declaration: 73-meric	Chain BB 1–450（450 aa） Chain CB 1–450（450 aa） Chain DB 1–450（450 aa） Chain EB 1–450（450 aa） Chain FB 1–450（450 aa） Chain GB 1–450（450 aa） Chain HB 1–450（450 aa） Chain IB 1–450（450 aa） Chain JB 1–450（450 aa） Chain KB 1–450（450 aa） Chain LB 1–450（450 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	GTP GUANOSINE-5'-TRIPHOSPHATE × 11	ELECTRON MICROSCOPY cryo-EM buffer pH 6.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.67 Å
9WD7 GMPCPP-stabilizsd human alpha1A/beta3 microtubule Deposited 2025-08-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain b 1–450（450 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.34 Å
9WD9 GMPCPP-stabilized human alpha1A/beta3 S239C microtubule Deposited 2025-08-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain b 1–450（450 aa）	Mutation：S239C	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.26 Å
9WDA Paclitaxel/GMPCPP-stabilized human alpha1A/beta3 microtubule Deposited 2025-08-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain b 1–450（450 aa）	Not recorded	MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 TA1 TAXOL × 1 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.35 Å
9WDB Paclitaxel/GMPCPP-stabilized human alpha1A/beta3 S239C microtubule Deposited 2025-08-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain b 1–450（450 aa）	Mutation：S239c	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 TA1 TAXOL × 1 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.39 Å

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TBB3_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain C； PDBConstruct 1–426； UniProt 1–426 Author chain D； PDBConstruct 1–426； UniProt 1–426 Author chain I； PDBConstruct 1–426； UniProt 1–426 Author chain J； PDBConstruct 1–426； UniProt 1–426 Author chain K； PDBConstruct 1–426； UniProt 1–426 Author chain L； PDBConstruct 1–426； UniProt 1–426

Tubulin alpha-1A chain

Homo sapiens

UniProt Q71U36

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 × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain A； UniProt 1–437 Chain B； UniProt 1–437 Chain E； UniProt 1–437 Chain F； UniProt 1–437 Chain G； UniProt 1–437 Chain H； UniProt 1–437	Not recorded	Tubulin beta-3 chain × 6 （Q13509） G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 6 MG MAGNESIUM ION × 12 GTP GUANOSINE-5'-TRIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer：pH 6.9 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.00 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 5JCO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
22AJ GDP human alpha1A/beta3 S239C microtubule Deposited 2026-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–451（451 aa）	Not recorded	MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.48 Å
22AK GDP human alpha1A/beta3 microtubule Deposited 2026-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–451（451 aa）	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.41 Å
6WSL Cryo-EM structure of VASH1-SVBP bound to microtubules Deposited 2020-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–451（451 aa） Chain E 1–451（451 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
7UN1 8-nm repeat of the human sperm tip singlet microtubule Deposited 2022-04-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 109 PDB declaration: 109-meric	Chain AC 1–451（451 aa） Chain AE 1–451（451 aa） Chain BC 1–451（451 aa） Chain BE 1–451（451 aa） Chain BG 1–451（451 aa） Chain CC 1–451（451 aa） Chain CE 1–451（451 aa） Chain CG 1–451（451 aa） Chain DC 1–451（451 aa） Chain DE 1–451（451 aa） Chain DG 1–451（451 aa） Chain EC 1–451（451 aa） Chain EE 1–451（451 aa） Chain EG 1–451（451 aa） Chain FC 1–451（451 aa） Chain FE 1–451（451 aa） Chain FG 1–451（451 aa） Chain GC 1–451（451 aa） Chain GE 1–451（451 aa） Chain GG 1–451（451 aa） Chain HC 1–451（451 aa） Chain HE 1–451（451 aa） Chain HG 1–451（451 aa） Chain IC 1–451（451 aa） Chain IE 1–451（451 aa） Chain IG 1–451（451 aa） Chain JC 1–451（451 aa） Chain JE 1–451（451 aa） Chain JG 1–451（451 aa） Chain KC 1–451（451 aa） Chain KE 1–451（451 aa） Chain KG 1–451（451 aa） Chain LA 1–451（451 aa） Chain LC 1–451（451 aa） Chain LE 1–451（451 aa） Chain MA 1–451（451 aa） Chain MC 1–451（451 aa） Chain ME 1–451（451 aa）	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 38 GTP GUANOSINE-5'-TRIPHOSPHATE × 38 MG MAGNESIUM ION × 38	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.00 Å
7UNG 48-nm repeat of the human respiratory doublet microtubule Deposited 2022-04-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 435 PDB declaration: 435-meric	Chain AA 1–451（451 aa） Chain AC 1–451（451 aa） Chain AE 1–451（451 aa） Chain AG 1–451（451 aa） Chain AI 1–451（451 aa） Chain AK 1–451（451 aa） Chain AM 1–451（451 aa） Chain BA 1–451（451 aa） Chain BC 1–451（451 aa） Chain BE 1–451（451 aa） Chain BG 1–451（451 aa） Chain BI 1–451（451 aa） Chain BK 1–451（451 aa） Chain BM 1–451（451 aa） Chain CA 1–451（451 aa） Chain CC 1–451（451 aa） Chain CE 1–451（451 aa） Chain CG 1–451（451 aa） Chain CI 1–451（451 aa） Chain CK 1–451（451 aa） Chain CM 1–451（451 aa） Chain DA 1–451（451 aa） Chain DC 1–451（451 aa） Chain DE 1–451（451 aa） Chain DG 1–451（451 aa） Chain DI 1–451（451 aa） Chain DK 1–451（451 aa） Chain DM 1–451（451 aa） Chain EC 1–451（451 aa） Chain EE 1–451（451 aa） Chain EG 1–451（451 aa） Chain EI 1–451（451 aa） Chain EK 1–451（451 aa） Chain EM 1–451（451 aa） Chain FC 1–451（451 aa） Chain FE 1–451（451 aa） Chain FG 1–451（451 aa） Chain FI 1–451（451 aa） Chain FK 1–451（451 aa） Chain FM 1–451（451 aa） Chain GC 1–451（451 aa） Chain GE 1–451（451 aa） Chain GG 1–451（451 aa） Chain GI 1–451（451 aa） Chain GK 1–451（451 aa） Chain GM 1–451（451 aa） Chain HC 1–451（451 aa） Chain HE 1–451（451 aa） Chain HG 1–451（451 aa） Chain HI 1–451（451 aa） Chain HK 1–451（451 aa） Chain HM 1–451（451 aa） Chain HO 1–451（451 aa） Chain IC 1–451（451 aa） Chain IE 1–451（451 aa） Chain IG 1–451（451 aa） Chain II 1–451（451 aa） Chain IK 1–451（451 aa） Chain IM 1–451（451 aa） Chain IO 1–451（451 aa） Chain JC 1–451（451 aa） Chain JE 1–451（451 aa） Chain JG 1–451（451 aa） Chain JI 1–451（451 aa） Chain JK 1–451（451 aa） Chain JM 1–451（451 aa） Chain KC 1–451（451 aa） Chain KE 1–451（451 aa） Chain KG 1–451（451 aa） Chain KI 1–451（451 aa） Chain KK 1–451（451 aa） Chain KM 1–451（451 aa） Chain KO 1–451（451 aa） Chain LC 1–451（451 aa） Chain LE 1–451（451 aa） Chain LG 1–451（451 aa） Chain LI 1–451（451 aa） Chain LK 1–451（451 aa） Chain LM 1–451（451 aa） Chain MC 1–451（451 aa） Chain ME 1–451（451 aa） Chain MG 1–451（451 aa） Chain MI 1–451（451 aa） Chain MK 1–451（451 aa） Chain MM 1–451（451 aa） Chain NC 1–451（451 aa） Chain NE 1–451（451 aa） Chain NG 1–451（451 aa） Chain NI 1–451（451 aa） Chain NK 1–451（451 aa） Chain NM 1–451（451 aa） Chain OC 1–451（451 aa） Chain OE 1–451（451 aa） Chain OG 1–451（451 aa） Chain OI 1–451（451 aa） Chain OK 1–451（451 aa） Chain OM 1–451（451 aa） Chain OO 1–451（451 aa） Chain PC 1–451（451 aa） Chain PE 1–451（451 aa） Chain PG 1–451（451 aa） Chain PI 1–451（451 aa） Chain PK 1–451（451 aa） Chain PM 1–451（451 aa） Chain PO 1–451（451 aa） Chain QC 1–451（451 aa） Chain QE 1–451（451 aa） Chain QG 1–451（451 aa） Chain QI 1–451（451 aa） Chain QK 1–451（451 aa） Chain QM 1–451（451 aa） Chain QO 1–451（451 aa） Chain RC 1–451（451 aa） Chain RE 1–451（451 aa） Chain RG 1–451（451 aa） Chain RI 1–451（451 aa） Chain RK 1–451（451 aa） Chain RM 1–451（451 aa） Chain RO 1–451（451 aa） Chain SE 1–451（451 aa） Chain SG 1–451（451 aa） Chain SI 1–451（451 aa） Chain SK 1–451（451 aa） Chain SM 1–451（451 aa） Chain SO 1–451（451 aa） Chain TE 1–451（451 aa） Chain TG 1–451（451 aa） Chain TI 1–451（451 aa） Chain TK 1–451（451 aa） Chain TM 1–451（451 aa） Chain TO 1–451（451 aa） Chain UE 1–451（451 aa） Chain UG 1–451（451 aa） Chain UI 1–451（451 aa） Chain UK 1–451（451 aa） Chain UM 1–451（451 aa） Chain UO 1–451（451 aa） Chain VE 1–451（451 aa） Chain VG 1–451（451 aa） Chain VI 1–451（451 aa） Chain VK 1–451（451 aa） Chain VM 1–451（451 aa） Chain VO 1–451（451 aa） Chain WE 1–451（451 aa） Chain WG 1–451（451 aa） Chain WI 1–451（451 aa） Chain WK 1–451（451 aa） Chain WM 1–451（451 aa） Chain WO 1–451（451 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 149 MG MAGNESIUM ION × 149 GDP GUANOSINE-5'-DIPHOSPHATE × 153	ELECTRON MICROSCOPY cryo-EM buffer pH 7.3 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
8J07 96nm repeat of human respiratory doublet microtubule and associated axonemal complexes Deposited 2023-04-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 974 PDB declaration: 974-meric	Chain AC 1–451（451 aa） Chain AE 1–451（451 aa） Chain AG 1–451（451 aa） Chain AI 1–451（451 aa） Chain AK 1–451（451 aa） Chain AM 1–451（451 aa） Chain AO 1–451（451 aa） Chain AQ 1–451（451 aa） Chain AS 1–451（451 aa） Chain AU 1–451（451 aa） Chain AW 1–451（451 aa） Chain AY 1–451（451 aa） Chain AZ 1–451（451 aa） Chain BA 1–451（451 aa） Chain BC 1–451（451 aa） Chain BE 1–451（451 aa） Chain BG 1–451（451 aa） Chain BI 1–451（451 aa） Chain BK 1–451（451 aa） Chain BM 1–451（451 aa） Chain BO 1–451（451 aa） Chain BQ 1–451（451 aa） Chain BS 1–451（451 aa） Chain BU 1–451（451 aa） Chain BW 1–451（451 aa） Chain BY 1–451（451 aa） Chain CC 1–451（451 aa） Chain CE 1–451（451 aa） Chain CG 1–451（451 aa） Chain CI 1–451（451 aa） Chain CK 1–451（451 aa） Chain CM 1–451（451 aa） Chain CO 1–451（451 aa） Chain CQ 1–451（451 aa） Chain CS 1–451（451 aa） Chain CU 1–451（451 aa） Chain CW 1–451（451 aa） Chain CY 1–451（451 aa） Chain DC 1–451（451 aa） Chain DE 1–451（451 aa） Chain DG 1–451（451 aa） Chain DI 1–451（451 aa） Chain DK 1–451（451 aa） Chain DM 1–451（451 aa） Chain DO 1–451（451 aa） Chain DQ 1–451（451 aa） Chain DS 1–451（451 aa） Chain DU 1–451（451 aa） Chain DW 1–451（451 aa） Chain DY 1–451（451 aa） Chain EC 1–451（451 aa） Chain EE 1–451（451 aa） Chain EG 1–451（451 aa） Chain EI 1–451（451 aa） Chain EK 1–451（451 aa） Chain EM 1–451（451 aa） Chain EO 1–451（451 aa） Chain EQ 1–451（451 aa） Chain ES 1–451（451 aa） Chain EU 1–451（451 aa） Chain EW 1–451（451 aa） Chain EY 1–451（451 aa） Chain FC 1–451（451 aa） Chain FE 1–451（451 aa） Chain FG 1–451（451 aa） Chain FI 1–451（451 aa） Chain FK 1–451（451 aa） Chain FM 1–451（451 aa） Chain FO 1–451（451 aa） Chain FQ 1–451（451 aa） Chain FS 1–451（451 aa） Chain FU 1–451（451 aa） Chain FW 1–451（451 aa） Chain FY 1–451（451 aa） Chain GC 1–451（451 aa） Chain GE 1–451（451 aa） Chain GG 1–451（451 aa） Chain GI 1–451（451 aa） Chain GK 1–451（451 aa） Chain GM 1–451（451 aa） Chain GO 1–451（451 aa） Chain GQ 1–451（451 aa） Chain GS 1–451（451 aa） Chain GU 1–451（451 aa） Chain GW 1–451（451 aa） Chain GY 1–451（451 aa） Chain HA 1–451（451 aa） Chain HC 1–451（451 aa） Chain HE 1–451（451 aa） Chain HG 1–451（451 aa） Chain HI 1–451（451 aa） Chain HK 1–451（451 aa） Chain HM 1–451（451 aa） Chain HO 1–451（451 aa） Chain HQ 1–451（451 aa） Chain HS 1–451（451 aa） Chain HU 1–451（451 aa） Chain HW 1–451（451 aa） Chain HY 1–451（451 aa） Chain IA 1–451（451 aa） Chain IC 1–451（451 aa） Chain IE 1–451（451 aa） Chain IG 1–451（451 aa） Chain II 1–451（451 aa） Chain IK 1–451（451 aa） Chain IM 1–451（451 aa） Chain IO 1–451（451 aa） Chain IQ 1–451（451 aa） Chain IS 1–451（451 aa） Chain IU 1–451（451 aa） Chain IW 1–451（451 aa） Chain IY 1–451（451 aa） Chain JC 1–451（451 aa） Chain JE 1–451（451 aa） Chain JG 1–451（451 aa） Chain JI 1–451（451 aa） Chain JK 1–451（451 aa） Chain JM 1–451（451 aa） Chain JO 1–451（451 aa） Chain JQ 1–451（451 aa） Chain JS 1–451（451 aa） Chain JU 1–451（451 aa） Chain JW 1–451（451 aa） Chain JY 1–451（451 aa） Chain KC 1–451（451 aa） Chain KE 1–451（451 aa） Chain KG 1–451（451 aa） Chain KI 1–451（451 aa） Chain KK 1–451（451 aa） Chain KM 1–451（451 aa） Chain KO 1–451（451 aa） Chain KQ 1–451（451 aa） Chain KS 1–451（451 aa） Chain KU 1–451（451 aa） Chain KW 1–451（451 aa） Chain KY 1–451（451 aa） Chain LC 1–451（451 aa） Chain LE 1–451（451 aa） Chain LG 1–451（451 aa） Chain LI 1–451（451 aa） Chain LK 1–451（451 aa） Chain LM 1–451（451 aa） Chain LO 1–451（451 aa） Chain LQ 1–451（451 aa） Chain LS 1–451（451 aa） Chain LU 1–451（451 aa） Chain LW 1–451（451 aa） Chain LY 1–451（451 aa） Chain MA 1–451（451 aa） Chain MC 1–451（451 aa） Chain ME 1–451（451 aa） Chain MG 1–451（451 aa） Chain MI 1–451（451 aa） Chain MK 1–451（451 aa） Chain MM 1–451（451 aa） Chain MO 1–451（451 aa） Chain MQ 1–451（451 aa） Chain MS 1–451（451 aa） Chain MU 1–451（451 aa） Chain MW 1–451（451 aa） Chain MY 1–451（451 aa） Chain NA 1–451（451 aa） Chain NC 1–451（451 aa） Chain NE 1–451（451 aa） Chain NG 1–451（451 aa） Chain NI 1–451（451 aa） Chain NK 1–451（451 aa） Chain NM 1–451（451 aa） Chain NO 1–451（451 aa） Chain NQ 1–451（451 aa） Chain NS 1–451（451 aa） Chain NU 1–451（451 aa） Chain NW 1–451（451 aa） Chain OA 1–451（451 aa） Chain OC 1–451（451 aa） Chain OE 1–451（451 aa） Chain OG 1–451（451 aa） Chain OI 1–451（451 aa） Chain OK 1–451（451 aa） Chain OM 1–451（451 aa） Chain OO 1–451（451 aa） Chain OQ 1–451（451 aa） Chain OS 1–451（451 aa） Chain OU 1–451（451 aa） Chain OW 1–451（451 aa） Chain OY 1–451（451 aa） Chain PA 1–451（451 aa） Chain PC 1–451（451 aa） Chain PE 1–451（451 aa） Chain PG 1–451（451 aa） Chain PI 1–451（451 aa） Chain PK 1–451（451 aa） Chain PM 1–451（451 aa） Chain PO 1–451（451 aa） Chain PQ 1–451（451 aa） Chain PS 1–451（451 aa） Chain PU 1–451（451 aa） Chain PW 1–451（451 aa） Chain PY 1–451（451 aa） Chain QA 1–451（451 aa） Chain QC 1–451（451 aa） Chain QE 1–451（451 aa） Chain QG 1–451（451 aa） Chain QI 1–451（451 aa） Chain QK 1–451（451 aa） Chain QM 1–451（451 aa） Chain QO 1–451（451 aa） Chain QQ 1–451（451 aa） Chain QS 1–451（451 aa） Chain QU 1–451（451 aa） Chain QW 1–451（451 aa） Chain QY 1–451（451 aa） Chain RA 1–451（451 aa） Chain RC 1–451（451 aa） Chain RE 1–451（451 aa） Chain RG 1–451（451 aa） Chain RI 1–451（451 aa） Chain RK 1–451（451 aa） Chain RM 1–451（451 aa） Chain RO 1–451（451 aa） Chain RQ 1–451（451 aa） Chain RS 1–451（451 aa） Chain RU 1–451（451 aa） Chain RW 1–451（451 aa） Chain RY 1–451（451 aa） Chain SC 1–451（451 aa） Chain SE 1–451（451 aa） Chain SG 1–451（451 aa） Chain SI 1–451（451 aa） Chain SK 1–451（451 aa） Chain SM 1–451（451 aa） Chain SO 1–451（451 aa） Chain SQ 1–451（451 aa） Chain SS 1–451（451 aa） Chain SU 1–451（451 aa） Chain SW 1–451（451 aa） Chain SY 1–451（451 aa） Chain TC 1–451（451 aa） Chain TE 1–451（451 aa） Chain TG 1–451（451 aa） Chain TI 1–451（451 aa） Chain TK 1–451（451 aa） Chain TM 1–451（451 aa） Chain TO 1–451（451 aa） Chain TQ 1–451（451 aa） Chain TS 1–451（451 aa） Chain TU 1–451（451 aa） Chain TW 1–451（451 aa） Chain TY 1–451（451 aa） Chain UC 1–451（451 aa） Chain UE 1–451（451 aa） Chain UG 1–451（451 aa） Chain UI 1–451（451 aa） Chain UK 1–451（451 aa） Chain UM 1–451（451 aa） Chain UO 1–451（451 aa） Chain UQ 1–451（451 aa） Chain US 1–451（451 aa） Chain UU 1–451（451 aa） Chain UW 1–451（451 aa） Chain UY 1–451（451 aa） Chain VC 1–451（451 aa） Chain VE 1–451（451 aa） Chain VG 1–451（451 aa） Chain VI 1–451（451 aa） Chain VK 1–451（451 aa） Chain VM 1–451（451 aa） Chain VO 1–451（451 aa） Chain VQ 1–451（451 aa） Chain VS 1–451（451 aa） Chain VU 1–451（451 aa） Chain VW 1–451（451 aa） Chain VY 1–451（451 aa） Chain WA 1–451（451 aa） Chain WC 1–451（451 aa） Chain WE 1–451（451 aa） Chain WG 1–451（451 aa） Chain WI 1–451（451 aa） Chain WK 1–451（451 aa） Chain WM 1–451（451 aa） Chain WO 1–451（451 aa） Chain WQ 1–451（451 aa） Chain WS 1–451（451 aa） Chain WU 1–451（451 aa） Chain WW 1–451（451 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 285 MG MAGNESIUM ION × 285 GDP GUANOSINE-5'-DIPHOSPHATE × 289	ELECTRON MICROSCOPY cryo-EM buffer pH 7.3 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.10 Å
8SH7 TUBB4B and TUBA1A Heterodimer from Human Respiratory Doublet Microtubules Deposited 2023-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–451（451 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.3 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
9OX7 In situ microtubule structure in the axon of a human neuron Deposited 2025-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–451（451 aa） Chain C 1–451（451 aa） Chain G 1–451（451 aa） Chain H 1–451（451 aa）	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 4 GTP GUANOSINE-5'-TRIPHOSPHATE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.69 Å
9WD7 GMPCPP-stabilizsd human alpha1A/beta3 microtubule Deposited 2025-08-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain a 1–451（451 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.34 Å
9WD9 GMPCPP-stabilized human alpha1A/beta3 S239C microtubule Deposited 2025-08-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain a 1–451（451 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.26 Å
9WDA Paclitaxel/GMPCPP-stabilized human alpha1A/beta3 microtubule Deposited 2025-08-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain a 1–451（451 aa）	Not recorded	MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 TA1 TAXOL × 1 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.35 Å
9WDB Paclitaxel/GMPCPP-stabilized human alpha1A/beta3 S239C microtubule Deposited 2025-08-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain a 1–451（451 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 TA1 TAXOL × 1 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.39 Å

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TBA1A_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A； PDBConstruct 1–437； UniProt 1–437 Author chain B； PDBConstruct 1–437； UniProt 1–437 Author chain E； PDBConstruct 1–437； UniProt 1–437 Author chain F； PDBConstruct 1–437； UniProt 1–437 Author chain G； PDBConstruct 1–437； UniProt 1–437 Author chain H； PDBConstruct 1–437； UniProt 1–437

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	5jco
Deposition date deposition_date	2016-04-15
Structure title title	Structure and dynamics of single-isoform recombinant neuronal human tubulin
Keywords keywords	microtubules, tubulin, single isoform, recombinant, dynamic instability, 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	66.56 Å
Radius of gyration Rg (electron density) rg_electron	66.60 Å
Forward intensity I(0) i0	4889630000.00
Molecular weight molecular_weight	577280.0 kDa
Excluded volume excluded_volume	715580 Å³
Envelope volume envelope_volume	1009900 Å³
Hydration-shell volume shell_volume	125310 Å³
Envelope diameter envelope_diameter	238.6 Å
Shell Rg shell_rg	66.14 Å
Envelope Rg envelope_rg	65.51 Å
Shape Rg shape_rg	66.60 Å
Total Rg total_rg	66.57 Å
Total atoms total_atoms	40512
Residues n_residues	5124
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	228.2 Å
Rg (real space) rg_real	66.59 Å
Rg uncertainty (real space) rg_real_error	2.24 Å
I(0) (real space) i0_real	4.8900e+09
I(0) uncertainty (real space) i0_real_error	1.1830e+08
Rg (reciprocal space) rg_reciprocal	66.46 Å
I(0) (reciprocal space) i0_reciprocal	4888000000.0000
Solution quality estimate total_estimate	0.8758
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	76.1 Å
Skewness Skewness skewness	0.251
Kurtosis Kurtosis kurtosis	-0.520
Angular range angular_range	— – 0.1200 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	161600000.0000
Real-space data points n_real_points	25
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.769

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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	Tubulin beta-3 chain
Molecular weight formula_weight	47809.9 kDa
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	K,I,J,C,D,L
Atom count atom_count	40512

MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYVPRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQ

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Spodoptera frugiperda

Entity 2 Entity 2 polymer

Description description	Tubulin alpha-1A chain
Molecular weight formula_weight	48649.0 kDa
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,E,F,A,B,G

MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGV

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Spodoptera frugiperda

Entity 3 Entity 3 non-polymer

Description description	PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER
Molecular weight formula_weight	521.2 kDa
Source method src_method	man
Copy count entity_count	6

Entity 4 Entity 4 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	man
Copy count entity_count	12

Entity 5 Entity 5 non-polymer

Description description	GUANOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	523.2 kDa
Source method src_method	man
Copy count entity_count	6

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7. Fold Classification (SCOP + CATH) 36 domains

CATH v4.4 (36 domains)

Domain ID domain_id	5jcoA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1440 — Tubulin/FtsZ, GTPase domain

Domain ID domain_id	5jcoA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	20 — Tubulin/FtsZ, C-terminal domain

Domain ID domain_id	5jcoA03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	600 — Helix hairpin bin

Domain ID domain_id	5jcoB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1440 — Tubulin/FtsZ, GTPase domain

Domain ID domain_id	5jcoB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	20 — Tubulin/FtsZ, C-terminal domain

Domain ID domain_id	5jcoB03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	600 — Helix hairpin bin

Domain ID domain_id	5jcoC01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1440 — Tubulin/FtsZ, GTPase domain

Domain ID domain_id	5jcoC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	20 — Tubulin/FtsZ, C-terminal domain

Domain ID domain_id	5jcoC03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	600 — Helix hairpin bin

Domain ID domain_id	5jcoD01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1440 — Tubulin/FtsZ, GTPase domain

Domain ID domain_id	5jcoD02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	20 — Tubulin/FtsZ, C-terminal domain

Domain ID domain_id	5jcoD03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	600 — Helix hairpin bin

Domain ID domain_id	5jcoE01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1440 — Tubulin/FtsZ, GTPase domain

Domain ID domain_id	5jcoE02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	20 — Tubulin/FtsZ, C-terminal domain

Domain ID domain_id	5jcoE03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	600 — Helix hairpin bin

Domain ID domain_id	5jcoF01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1440 — Tubulin/FtsZ, GTPase domain

Domain ID domain_id	5jcoF02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	20 — Tubulin/FtsZ, C-terminal domain

Domain ID domain_id	5jcoF03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	600 — Helix hairpin bin

Domain ID domain_id	5jcoG01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1440 — Tubulin/FtsZ, GTPase domain

Domain ID domain_id	5jcoG02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	20 — Tubulin/FtsZ, C-terminal domain

Domain ID domain_id	5jcoG03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	600 — Helix hairpin bin

Domain ID domain_id	5jcoH01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1440 — Tubulin/FtsZ, GTPase domain

Domain ID domain_id	5jcoH02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	20 — Tubulin/FtsZ, C-terminal domain

Domain ID domain_id	5jcoH03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	600 — Helix hairpin bin

Domain ID domain_id	5jcoI01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1440 — Tubulin/FtsZ, GTPase domain

Domain ID domain_id	5jcoI02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	20 — Tubulin/FtsZ, C-terminal domain

Domain ID domain_id	5jcoI03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	600 — Helix hairpin bin

Domain ID domain_id	5jcoJ01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1440 — Tubulin/FtsZ, GTPase domain

Domain ID domain_id	5jcoJ02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	20 — Tubulin/FtsZ, C-terminal domain

Domain ID domain_id	5jcoJ03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	600 — Helix hairpin bin

Domain ID domain_id	5jcoK01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1440 — Tubulin/FtsZ, GTPase domain

Domain ID domain_id	5jcoK02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	20 — Tubulin/FtsZ, C-terminal domain

Domain ID domain_id	5jcoK03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	600 — Helix hairpin bin

Domain ID domain_id	5jcoL01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1440 — Tubulin/FtsZ, GTPase domain

Domain ID domain_id	5jcoL02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	20 — Tubulin/FtsZ, C-terminal domain

Domain ID domain_id	5jcoL03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	600 — Helix hairpin bin

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8. Citations (1)

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

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

Resolution resolution	4.000 Å
Low-resolution limit resolution_low	214.900 Å
R factor r_factor	0.3793
R_work r_work	0.3793
R_free r_free	—

Resolution resolution	4.00 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	10164

Structure and dynamics of single-isoform recombinant neuronal human tubulin

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

Tubulin beta-3 chain

State in the Current Structure

Other States of the Same Protein in the Database

Tubulin alpha-1A chain

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

7. Fold Classification (SCOP + CATH) 36 domains

CATH v4.4 (36 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/jc/5jco/5jco.fit
pddf	/app/data/pr_computation/jc/5jco/5jco.pr.out
profile	/app/data/saxs_computation/jc/5jco/5jco.dat