Research workbench
Crystal structure of mtor docked into EM MAP of dimeric atm kinase
Analyse Crystal structure of mtor docked into EM MAP of dimeric atm kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JBZ
- Type
- protein
- Length
- 960 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase mtor
- EC
- 2.7.11.1
- UniProt
- P42345
- Ligands
- ADP, MGF, MG
- Pockets
- 13 · best druggability 0.78
Structure
electron microscopy · 1 distinct chain · 65% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase mtor (EC 2.7.11.1) | protein | 960 | 65% helix, 5% strand | P42345 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MGF · Trifluoromagnesate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1138 | 0.78 | 0.79 | 83 | empty |
| 2 | 727 | 0.75 | 0.80 | 54 | empty |
| 3 | 626 | 0.69 | 0.77 | 56 | empty |
| 4 | 146 | 0.68 | 0.88 | 28 | empty |
| 5 | 225 | 0.57 | 0.79 | 26 | ADP, MG |
Compared structures
- 3JBZ · Crystal structure of mTOR docked into EM map of dimeric ATM kinase · the same entry in another collection · chain A against A, TM-score 1.00
- P42345 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase mtor (P42345) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P42345
- Elsewhere: RCSB PDB 3JBZ · PDBe 3JBZ · UniProt P42345
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