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
- 3NWS
- Type
- protein
- Length
- 780 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division control protein 13
- UniProt
- P32797
- Pockets
- 17 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Cell division control protein 13 | protein | 195 | 30% helix, 27% strand | P32797 |
Pockets
17 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1023 | 0.75 | 0.78 | 69 | empty |
| 2 | 210 | 0.53 | 0.77 | 27 | empty |
| 3 | 107 | 0.51 | 0.82 | 33 | empty |
| 4 | 192 | 0.50 | 0.77 | 30 | empty |
| 5 | 204 | 0.50 | 0.76 | 31 | empty |
Interfaces
4 interfaces between chains.
- B–D · 1471 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 1449 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 616 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 72 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3NWS · Crystal structure of the N-terminal domain of the yeast telomere-binding and telomerase… · the same entry in another collection · chain D against D, 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 B against A, TM-score 0.98
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 3NWS · PDBe 3NWS · UniProt P32797
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