Research workbench
Structural basis for telomere length regulation by the shelterin bridge
Analyse Structural basis for telomere length regulation by the shelterin bridge in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WE2
- Type
- protein
- Length
- 525 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protection of telomeres protein POZ1; Protection of telomeres protein TPZ1; DNA-binding…
- UniProt
- O13852, O14246, Q96TL7
- Ligands
- ZN
- Pockets
- 7 · best druggability 0.55
Structure
x-ray diffraction · 5 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protection of telomeres protein POZ1 | protein | 229 | 72% helix, 0% strand | O13852 |
| B | Protection of telomeres protein TPZ1 | protein | 32 | 59% helix, 0% strand | O14246 |
| C | Protection of telomeres protein POZ1 | protein | 229 | 69% helix, 0% strand | O13852 |
| D | Protection of telomeres protein TPZ1 | protein | 29 | 69% helix, 0% strand | O14246 |
| F | DNA-binding protein RAP1 | protein | 6 | 0% helix, 0% strand | Q96TL7 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.55 | 0.81 | 24 | empty |
| 2 | 178 | 0.51 | 0.78 | 25 | empty |
| 3 | 210 | 0.49 | 0.76 | 30 | empty |
| 4 | 99 | 0.35 | 0.73 | 19 | empty |
| 5 | 51 | 0.30 | 0.77 | 11 | empty |
Interfaces
4 interfaces between chains.
- C–D · 1296 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1282 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 735 Ų buried · 13 hydrogen bonds · protein-protein
- C–F · 346 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5WE2 · Structural Basis for Telomere Length Regulation by the Shelterin Bridge · the same entry in another collection · chain F against F, TM-score 1.00
- O13852 · AlphaFold monomer V2.0 prediction for protection of telomeres protein POZ1 (O13852) · a predicted model of the same protein · chain A against A, TM-score 0.95
- O14246 · AlphaFold monomer V2.0 prediction for protection of telomeres protein TPZ1 (O14246) · a predicted model of the same protein · chain D against A, TM-score 0.61
- Q96TL7 · AlphaFold monomer V2.0 prediction for DNA-binding protein RAP1 (Q96TL7) · a predicted model of the same protein · chain F against A, TM-score 0.55
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 O13852
- Every structure of UniProt O14246
- Every structure of UniProt Q96TL7
- Elsewhere: RCSB PDB 5WE2 · PDBe 5WE2 · UniProt O13852 · UniProt O14246 · UniProt Q96TL7
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