Research workbench
Crystal structure of the dimerization domain of S. pombe TAZ1
Analyse Crystal structure of the dimerization domain of S. pombe TAZ1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZMK
- Type
- protein
- Length
- 71 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Telomere length regulator TAZ1
- UniProt
- P79005
Structure
x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Telomere length regulator TAZ1 | protein | 71 | 75% helix, 0% strand | P79005 |
Compared structures
- 4ZMK · Crystal structure of the dimerization domain of S. pombe Taz1 · the same entry in another collection · chain A against A, TM-score 1.00
- P79005 · AlphaFold monomer V2.0 prediction for telomere length regulator TAZ1 (P79005) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P79005
- Elsewhere: RCSB PDB 4ZMK · PDBe 4ZMK · UniProt P79005
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