MolNFT v1 · #73540 · protein
TEL2 structure and function in the HSP90-dependent maturation of mtor and atr complexes
3O4Z · Telomere length regulation protein TEL2: “TEL2 structure and function in the HSP90-dependent maturation of mtor and atr complexes”. X-ray diffraction, 20 pockets (best druggability 0.83). MolNFT v1 #73540 on GenesisL1: 3D structure…
- PDB
- 3O4Z
- Type
- protein
- Length
- 2,288 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Telomere length regulation protein TEL2
- UniProt
- P53038
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Telomere length regulation protein TEL2 | protein | 572 | 70% helix, 0% strand | P53038 |
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 947 | 0.83 | 0.84 | 92 | empty |
| 2 | 659 | 0.82 | 0.86 | 75 | empty |
| 3 | 606 | 0.73 | 0.81 | 75 | empty |
| 4 | 450 | 0.59 | 0.75 | 33 | empty |
| 5 | 440 | 0.59 | 0.75 | 40 | empty |
Interfaces
4 interfaces between chains.
- B–D · 1660 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 1626 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 1593 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 1580 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 3O4Z · Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes · the same entry in another collection · chain A against A, TM-score 1.00
- P53038 · AlphaFold monomer V2.0 prediction for telomere length regulation protein TEL2 (P53038) · a predicted model of the same protein · chain A against A, TM-score 0.71
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 P53038
- Elsewhere: RCSB PDB 3O4Z · PDBe 3O4Z · UniProt P53038
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