Research workbench
Crystal structure of the N-terminal domain of the yeast telomere- binding and telomerase regulatory protein CDC13
Analyse Crystal structure of the N-terminal domain of the yeast telomere- binding and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NWT
- Type
- protein
- Length
- 189 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division control protein 13
- UniProt
- P32797
- Pockets
- 2 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division control protein 13 | protein | 189 | 33% helix, 28% strand | P32797 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 53 | 0.35 | 0.79 | 16 | empty |
| 2 | 56 | 0.33 | 0.77 | 13 | empty |
Compared structures
- 3NWT · Crystal structure of the N-terminal domain of the yeast telomere-binding and telomerase… · the same entry in another collection · chain A against A, TM-score 1.00
- P32797 · AlphaFold monomer V2.0 prediction for cell division control protein 13 (P32797) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P32797
- Elsewhere: RCSB PDB 3NWT · PDBe 3NWT · UniProt P32797
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