2L3L: Tubulin-specific chaperone C

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.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
926
Mol. weight
13.17 kDa
Released
21 Sept 2011

Explore 2L3L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 6 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix32-376
α-helix40-434
α-helix49-557
α-helix56-7722
α-helix81-10020
α-helix107-13125

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tubulin-specific chaperone CAprotein111Homo sapiensQ15814 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2L3L_1 Tubulin-specific chaperone C (chains A)
MPERLQRREQERQLEVERRKQKRQNQEVEKENSHFFVATFARERAAVEELLERAESVERL
EEAASRLQGLQKLINDSVFFLAAYDLRQGQEALARLQAALAERRRGLQPKK

Primary citation

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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