Research workbench
Solution structure of the cap-gly domain in mouse tubulin specific chaperone B
Analyse Solution structure of the cap-gly domain in mouse tubulin specific chaperone B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WHG
- Type
- protein
- Length
- 113 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubulin specific chaperone B
- UniProt
- Q9D1E6
Structure
solution nmr · 1 distinct chain · 19% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubulin specific chaperone B | protein | 113 | 19% helix, 32% strand | Q9D1E6 |
Compared structures
- 1WHG · Solution structure of the CAP-Gly domain in mouse tubulin specific chaperone B · the same entry in another collection · chain A against A, TM-score 1.00
- Q9D1E6 · AlphaFold monomer V2.0 prediction for tubulin-folding cofactor B (Q9D1E6) · a predicted model of the same protein · chain A against A, TM-score 0.72
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 Q9D1E6
- Elsewhere: RCSB PDB 1WHG · PDBe 1WHG · UniProt Q9D1E6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.