Research workbench
Structure of the N-terminal domain of the yeast telomerase reverse transcriptase
Analyse Structure of the N-terminal domain of the yeast telomerase reverse transcriptase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NPT
- Type
- protein
- Length
- 125 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Telomerase reverse transcriptase
- UniProt
- R4IT35
- Pockets
- 2 · best druggability 0.30
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Telomerase reverse transcriptase | protein | 125 | 55% helix, 13% strand | R4IT35 |
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 | 50 | 0.30 | 0.77 | 19 | empty |
| 2 | 60 | 0.30 | 0.74 | 12 | empty |
Compared structures
- 5NPT · Structure of the N-terminal domain of the yeast telomerase reverse transcriptase · the same entry in another collection · chain A against A, TM-score 1.00
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 R4IT35
- Elsewhere: RCSB PDB 5NPT · PDBe 5NPT · UniProt R4IT35
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