Research workbench
The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for the interaction with ab- tubulin
Analyse The solution structure of the N-terminal domain of human tubulin binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2L3L
- Type
- protein
- Length
- 111 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubulin-specific chaperone C
- UniProt
- Q15814
Structure
solution nmr · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubulin-specific chaperone C | protein | 111 | 76% helix, 0% strand | Q15814 |
Compared structures
- 2L3L · The solution structure of the N-terminal domain of human Tubulin Binding Cofactor C… · the same entry in another collection · chain A against A, TM-score 1.00
- Q15814 · AlphaFold monomer V2.0 prediction for tubulin-specific chaperone C (Q15814) · a predicted model of the same protein · chain A against A, TM-score 0.68
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 Q15814
- Elsewhere: RCSB PDB 2L3L · PDBe 2L3L · UniProt Q15814
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