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Heterodimeric structure of ERK2 and RSK1
Analyse Heterodimeric structure of ERK2 and RSK1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NIF
- Type
- protein
- Length
- 1,323 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribosomal protein S6 kinase alpha-1; Mitogen-activated protein kinase 1
- EC
- 2.7.11.1, 2.7.11.24
- UniProt
- Q15418, P28482
- Ligands
- ANP, NA, SO4
- Pockets
- 17 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribosomal protein S6 kinase alpha-1 (EC 2.7.11.1) | protein | 313 | 42% helix, 17% strand | Q15418 |
| B | Mitogen-activated protein kinase 1 (EC 2.7.11.24) | protein | 349 | 37% helix, 14% strand | P28482 |
| D | Ribosomal protein S6 kinase alpha-1 (EC 2.7.11.1) | protein | 313 | 42% helix, 18% strand | Q15418 |
| E | Mitogen-activated protein kinase 1 (EC 2.7.11.24) | protein | 348 | 38% helix, 14% strand | P28482 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains B, E
- NA · Sodium ion · metal · 2 copies · chains B, E
- SO4 · Sulfate ion · ion · 3 copies · chains A, B, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 826 | 0.80 | 0.82 | 83 | ANP |
| 2 | 1105 | 0.79 | 0.81 | 106 | ANP |
| 3 | 430 | 0.71 | 0.82 | 62 | SO4, NA |
| 4 | 384 | 0.69 | 0.82 | 52 | SO4, NA |
| 5 | 255 | 0.66 | 0.83 | 31 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1566 Ų buried · 21 hydrogen bonds · protein-protein
- D–E · 1545 Ų buried · 21 hydrogen bonds · protein-protein
- A–D · 1090 Ų buried · 19 hydrogen bonds · protein-protein
- B–D · 357 Ų buried · 3 hydrogen bonds · protein-protein
- A–E · 357 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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 Q15418
- Every structure of UniProt P28482
- Elsewhere: RCSB PDB 4NIF · PDBe 4NIF · UniProt Q15418 · UniProt P28482
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