The solution structure of the N-terminal domain of human Tubulin Binding Cofactor C reveals a platform for the interaction with ab-tubulin. Determined by solution NMR. Released 21 Sept 2011.
Explore 2L3L in 3D Show helices and sheets RCSB PDB PDBe
2L3L contains 6 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 32-37 | 6 | |
| α-helix | 40-43 | 4 | |
| α-helix | 49-55 | 7 | |
| α-helix | 56-77 | 22 | |
| α-helix | 81-100 | 20 | |
| α-helix | 107-131 | 25 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tubulin-specific chaperone C | A | protein | 111 | Homo sapiens | Q15814 (AlphaFold model) |
>2L3L_1 Tubulin-specific chaperone C (chains A) MPERLQRREQERQLEVERRKQKRQNQEVEKENSHFFVATFARERAAVEELLERAESVERL EEAASRLQGLQKLINDSVFFLAAYDLRQGQEALARLQAALAERRRGLQPKK
The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction. Garcia-Mayoral, M.F., Castano, R., Lopez-Fanarraga, M.L. et al. To be published.
Other PDB entries of the same protein (UniProt Q15814 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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