Research workbench
Protelomerase telk complexed with substrate DNA
Analyse Protelomerase telk complexed with substrate DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V6E
- Type
- protein + DNA
- Length
- 1,150 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protelemorase; Telrl
- UniProt
- Q6UAV6
- Ligands
- VO4
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 55% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protelemorase | protein | 531 | 55% helix, 6% strand | Q6UAV6 |
| C, E | Telrl | dna | 25 | — | — |
| D, F | Telrl | dna | 19 | — | — |
Ligands and binding sites
- VO4 · Vanadate ion · ion · 2 copies · chains A, D, E, B, C, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1029 | 0.84 | 0.85 | 99 | empty |
| 2 | 1015 | 0.73 | 0.76 | 75 | empty |
| 3 | 967 | 0.72 | 0.76 | 73 | empty |
| 4 | 476 | 0.71 | 0.81 | 44 | empty |
| 5 | 406 | 0.70 | 0.82 | 37 | empty |
Interfaces
14 interfaces between chains.
- A–B · 2249 Ų buried · 42 hydrogen bonds · protein-protein
- B–E · 1545 Ų buried · 32 hydrogen bonds · protein-nucleic
- A–C · 1539 Ų buried · 32 hydrogen bonds · protein-nucleic
- A–D · 1289 Ų buried · 32 hydrogen bonds · protein-nucleic
- B–F · 1287 Ų buried · 31 hydrogen bonds · protein-nucleic
Compared structures
- 2V6E · protelomerase TelK complexed with substrate DNA · 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 Q6UAV6
- Elsewhere: RCSB PDB 2V6E · PDBe 2V6E · UniProt Q6UAV6
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