Research workbench
Crystal structure of the human EB1 C-terminal dimerization domain
Analyse Crystal structure of the human EB1 C-terminal dimerization domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YIB
- Type
- protein
- Length
- 61 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Microtubule-associated protein RP/EB family member 1
- UniProt
- Q15691
Structure
x-ray diffraction · 1 distinct chain · 87% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Microtubule-associated protein RP/EB family member 1 | protein | 61 | 87% helix, 0% strand | Q15691 |
Compared structures
- 1YIB · Crystal Structure of the Human EB1 C-terminal Dimerization Domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q15691 · AlphaFold monomer V2.0 prediction for microtubule-associated protein RP/EB family member… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q15691
- Elsewhere: RCSB PDB 1YIB · PDBe 1YIB · UniProt Q15691
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