Research workbench
PIH1D1/PHOSPHO-TEL2 complex
Analyse PIH1D1/PHOSPHO-TEL2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PSI
- Type
- protein
- Length
- 269 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PIH1 domain-containing protein 1; Telomere length regulation protein TEL2 homolog
- UniProt
- Q9NWS0, Q9Y4R8
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 4 distinct chains · 20% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PIH1 domain-containing protein 1 | protein | 125 | 22% helix, 35% strand | Q9NWS0 |
| B | PIH1 domain-containing protein 1 | protein | 123 | 22% helix, 36% strand | Q9NWS0 |
| D | Telomere length regulation protein TEL2 homolog | protein | 11 | 0% helix, 0% strand | Q9Y4R8 |
| E | Telomere length regulation protein TEL2 homolog | protein | 10 | 0% helix, 0% strand | Q9Y4R8 |
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 | 97 | 0.40 | 0.77 | 23 | empty |
| 2 | 73 | 0.34 | 0.76 | 18 | empty |
Interfaces
5 interfaces between chains.
- A–D · 650 Ų buried · 17 hydrogen bonds · protein-protein
- B–E · 635 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 567 Ų buried · 2 hydrogen bonds · protein-protein
- A–E · 13 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 11 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered, phosphorylation).
Compared structures
- 4PSI · PIH1D1/phospho-Tel2 complex · the same entry in another collection · chain E against E, TM-score 1.00
- Q9NWS0 · AlphaFold monomer V2.0 prediction for PIH1 domain-containing protein 1 (Q9NWS0) · a predicted model of the same protein · chain B against A, TM-score 0.89
- Q9Y4R8 · AlphaFold monomer V2.0 prediction for telomere length regulation protein TEL2 homolog… · a predicted model of the same protein · chain E against A, TM-score 0.45
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 Q9NWS0
- Every structure of UniProt Q9Y4R8
- Elsewhere: RCSB PDB 4PSI · PDBe 4PSI · UniProt Q9NWS0 · UniProt Q9Y4R8
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