Research workbench
Crystal structure of POZ1, TPZ1 and RAP1
Analyse Crystal structure of POZ1, TPZ1 and RAP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XXF
- Type
- protein
- Length
- 547 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protection of telomeres protein POZ1; Protection of telomeres protein TPZ1; RAP1
- UniProt
- O13852, O14246
- Ligands
- ZN
- Pockets
- 7 · best druggability 0.59
Structure
x-ray diffraction · 4 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protection of telomeres protein POZ1 | protein | 222 | 72% helix, 0% strand | O13852 |
| C, D | Protection of telomeres protein TPZ1 | protein | 31 | 65% helix, 0% strand | O14246 |
| E, F | RAP1 | protein | 17 | 0% helix, 0% strand | — |
| B | Protection of telomeres protein POZ1 | protein | 229 | 71% helix, 0% strand | O13852 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, C, B, 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 | 91 | 0.59 | 0.87 | 20 | empty |
| 2 | 123 | 0.58 | 0.84 | 25 | empty |
| 3 | 85 | 0.44 | 0.79 | 17 | empty |
| 4 | 97 | 0.39 | 0.76 | 22 | empty |
| 5 | 75 | 0.34 | 0.76 | 14 | empty |
Interfaces
5 interfaces between chains.
- B–D · 1267 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 1262 Ų buried · 14 hydrogen bonds · protein-protein
- B–F · 832 Ų buried · 8 hydrogen bonds · protein-protein
- A–E · 785 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 765 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 5XXF · Crystal structure of Poz1, Tpz1 and Rap1 · 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 0.97
- O14246 · AlphaFold monomer V2.0 prediction for protection of telomeres protein TPZ1 (O14246) · a predicted model of the same protein · chain C against A, TM-score 0.60
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
- Elsewhere: RCSB PDB 5XXF · PDBe 5XXF · UniProt O13852 · UniProt O14246
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