Tubulin alpha-1A chain
Mus musculus
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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count | Chain A; UniProt 1–451 Chain B; UniProt 1–451 Chain C; UniProt 1–451 Chain D; UniProt 1–451 Chain E; UniProt 1–451 Chain F; UniProt 1–451 Chain G; UniProt 1–451 Chain H; UniProt 1–451 Chain I; UniProt 1–451 | Not recorded | Tubulin beta-2A chain × 9 (Q7TMM9) Kinesin-1 heavy chain × 9 (P33176) GTP GUANOSINE-5'-TRIPHOSPHATE × 9 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 9 | ELECTRON MICROSCOPY cryo-EM buffer:pH 6.9 cryo-EM vitrification conditions:Cryogen ETHANE | Resolution 4.20 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 8IXA | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 8IXB GMPCPP-Alpha1A/Beta2A-microtubule decorated with kinesin seam region Deposited 2023-03-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion | Assembly 1 Protein heterocomplex Heteromer;Protein × 12 PDB declaration: dodecameric |
Chain A
1–451(451 aa)
Chain E
1–451(451 aa)
Chain F
1–451(451 aa)
Chain H
1–451(451 aa)
|
Not recorded | GTP GUANOSINE-5'-TRIPHOSPHATE × 4 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 6.9
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.20 Å |
| 8TO0 48-nm repeating structure of doublets from mouse sperm flagella Deposited 2023-08-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 471 PDB declaration: 471-meric |
Chain A5
1–451(451 aa)
Chain A7
1–451(451 aa)
Chain A9
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 Aj
1–451(451 aa)
Chain Al
1–451(451 aa)
Chain An
1–451(451 aa)
Chain Ap
1–451(451 aa)
Chain Ar
1–451(451 aa)
Chain At
1–451(451 aa)
Chain Av
1–451(451 aa)
Chain B0
1–451(451 aa)
Chain B2
1–451(451 aa)
Chain B4
1–451(451 aa)
Chain B8
1–451(451 aa)
Chain BA
1–451(451 aa)
Chain BC
1–451(451 aa)
Chain BE
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 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 Br
1–451(451 aa)
Chain Bt
1–451(451 aa)
Chain Bv
1–451(451 aa)
Chain Bx
1–451(451 aa)
Chain Bz
1–451(451 aa)
Chain C0
1–451(451 aa)
Chain C1
1–451(451 aa)
Chain C3
1–451(451 aa)
Chain C8
1–451(451 aa)
Chain CB
1–451(451 aa)
Chain CD
1–451(451 aa)
Chain CF
1–451(451 aa)
Chain CH
1–451(451 aa)
Chain CJ
1–451(451 aa)
Chain CN
1–451(451 aa)
Chain CP
1–451(451 aa)
Chain CR
1–451(451 aa)
Chain CT
1–451(451 aa)
Chain CV
1–451(451 aa)
Chain CX
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 Cs
1–451(451 aa)
Chain Cu
1–451(451 aa)
Chain Cw
1–451(451 aa)
Chain Cy
1–451(451 aa)
Chain D2
1–451(451 aa)
Chain D5
1–451(451 aa)
Chain D7
1–451(451 aa)
Chain D9
1–451(451 aa)
Chain DB
1–451(451 aa)
Chain DD
1–451(451 aa)
Chain DF
1–451(451 aa)
Chain DH
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 Db
1–451(451 aa)
Chain Dd
1–451(451 aa)
Chain Df
1–451(451 aa)
Chain Dh
1–451(451 aa)
Chain Dj
1–451(451 aa)
Chain Dl
1–451(451 aa)
Chain Dp
1–451(451 aa)
Chain Dr
1–451(451 aa)
Chain Dt
1–451(451 aa)
Chain Dv
1–451(451 aa)
Chain Dx
1–451(451 aa)
Chain Dz
1–451(451 aa)
Chain E3
1–451(451 aa)
Chain E5
1–451(451 aa)
Chain E7
1–451(451 aa)
Chain E9
1–451(451 aa)
Chain EA
1–451(451 aa)
Chain EC
1–451(451 aa)
Chain EE
1–451(451 aa)
Chain EG
1–451(451 aa)
Chain EJ
1–451(451 aa)
Chain EL
1–451(451 aa)
Chain EN
1–451(451 aa)
Chain EP
1–451(451 aa)
Chain ER
1–451(451 aa)
Chain ET
1–451(451 aa)
Chain EV
1–451(451 aa)
Chain EY
1–451(451 aa)
Chain Ea
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 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 FA
1–451(451 aa)
Chain FC
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 FU
1–451(451 aa)
Chain FW
1–451(451 aa)
Chain FY
1–451(451 aa)
Chain Fa
1–451(451 aa)
Chain Fc
1–451(451 aa)
Chain Fe
1–451(451 aa)
Chain N
1–451(451 aa)
Chain P
1–451(451 aa)
Chain R
1–451(451 aa)
Chain T
1–451(451 aa)
Chain V
1–451(451 aa)
Chain X
1–451(451 aa)
Chain Z
1–451(451 aa)
Chain n
1–451(451 aa)
Chain p
1–451(451 aa)
Chain r
1–451(451 aa)
Chain t
1–451(451 aa)
Chain v
1–451(451 aa)
Chain x
1–451(451 aa)
Chain z
1–451(451 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 7.70 Å |
| 9PND In situ microtubule of EpoB-induced regenerating axons Deposited 2025-07-20 | 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
1–451(451 aa)
Chain C
1–451(451 aa)
|
Not recorded | MG MAGNESIUM ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 2 EPB 7,11-DIHYDROXY-8,8,10,12,16-PENTAMETHYL-3-[1-METHYL-2-(2-METHYL-THIAZOL-4-YL)VINYL]-4,17-DIOXABICYCLO[14.1.0]HEPTADECANE-5,9-DIONE × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.2;Gibco Neurobasal Media
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.19 Å |
| 9SFP Native cytoplasmic lattices from mouse oocytes Deposited 2025-08-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions | Assembly 1 Protein heterocomplex Heteromer;Protein × 54 PDB declaration: 54-meric |
Chain a
1–451(451 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.2
cryo-EM vitrification conditions
Cryogen ETHANE-PROPANE
|
Resolution 4.20 Å |
| 9XRL Structure of mouse cytoplasmic lattice (CPL) repeating unit Deposited 2025-11-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 73 PDB declaration: 73-meric |
Chain AF
1–451(451 aa)
Chain AO
1–451(451 aa)
Chain u
1–451(451 aa)
|
Not recorded | ZN ZINC ION × 13 GTP GUANOSINE-5'-TRIPHOSPHATE × 5 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 3 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 6.7
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.74 Å |
5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | TBA1A_MOUSE |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 1–457; UniProt 1–451 Author chain B; PDBConstruct 1–457; UniProt 1–451 Author chain C; PDBConstruct 1–457; UniProt 1–451 Author chain D; PDBConstruct 1–457; UniProt 1–451 Author chain E; PDBConstruct 1–457; UniProt 1–451 Author chain F; PDBConstruct 1–457; UniProt 1–451 Author chain G; PDBConstruct 1–457; UniProt 1–451 Author chain H; PDBConstruct 1–457; UniProt 1–451 Author chain I; PDBConstruct 1–457; UniProt 1–451 |