Research workbench
Structure of alpha- and beta- tubulin in gmpcpp-microtubules
Analyse Structure of alpha- and beta- tubulin in gmpcpp-microtubules in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3J7I
- Type
- protein
- Length
- 820 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubulin alpha-1A chain; Tubulin beta chain
- UniProt
- P02550, P02554
- Ligands
- GTP, MG
- Pockets
- 14 · best druggability 0.87
Structure
electron microscopy · 2 distinct chains · 43% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubulin alpha-1A chain | protein | 409 | 43% helix, 14% strand | P02550 |
| B | Tubulin beta chain | protein | 411 | 43% helix, 12% strand | P02554 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 945 | 0.87 | 0.88 | 100 | GTP |
| 2 | 1002 | 0.78 | 0.80 | 87 | empty |
| 3 | 201 | 0.77 | 0.92 | 40 | empty |
| 4 | 804 | 0.72 | 0.77 | 73 | empty |
| 5 | 63 | 0.70 | 0.96 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1076 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P02550
- Every structure of UniProt P02554
- Elsewhere: RCSB PDB 3J7I · PDBe 3J7I · UniProt P02550 · UniProt P02554
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