MolNFT v1 · #49535 · protein
2.0A X-ray structure of C-terminal kinase domain of P90 ribosomal S6 kinase 2 (RSK2)
2QR8 · Ribosomal protein S6 kinase alpha-3: “2.0A X-ray structure of C-terminal kinase domain of P90 ribosomal S6 kinase 2 (RSK2)”. X-ray diffraction, 1 ligand (NA), 3 pockets (best druggability 0.61). MolNFT v1 #49535 on GenesisL1: 3D…
- PDB
- 2QR8
- Type
- protein
- Length
- 298 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribosomal protein S6 kinase alpha-3
- EC
- 2.7.11.1
- UniProt
- P18654
- Ligands
- NA
- Pockets
- 3 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribosomal protein S6 kinase alpha-3 (EC 2.7.11.1) | protein | 298 | 40% helix, 18% strand | P18654 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 334 | 0.61 | 0.78 | 31 | empty |
| 2 | 240 | 0.53 | 0.76 | 26 | empty |
| 3 | 133 | 0.43 | 0.76 | 27 | empty |
Compared structures
- 2QR8 · 2.0A X-ray structure of C-terminal kinase domain of p90 ribosomal S6 kinase 2 (RSK2) · the same entry in another collection · chain A against A, TM-score 1.00
- P18654 · AlphaFold monomer V2.0 prediction for ribosomal protein S6 kinase alpha-3 (P18654) · 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 P18654
- Elsewhere: RCSB PDB 2QR8 · PDBe 2QR8 · UniProt P18654
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