Research workbench
Crystal structure of murine receptor-interacting protein 4 (RIPK4) D143N bound to TG100-115
Analyse Crystal structure of murine receptor-interacting protein 4 (RIPK4) D143N bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WNK
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-interacting SERINE/THREONINE-protein kinase 4
- EC
- 2.7.11.1
- UniProt
- Q9ERK0
- Ligands
- B6J, CL
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-interacting SERINE/THREONINE-protein kinase 4 (EC 2.7.11.1) | protein | 263 | 41% helix, 16% strand | Q9ERK0 |
Ligands and binding sites
- B6J · 3,3'-(2,4-diaminopteridine-6,7-diyl)diphenol · ligand · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 273 | 0.63 | 0.80 | 27 | B6J |
| 2 | 78 | 0.43 | 0.80 | 15 | empty |
| 3 | 59 | 0.36 | 0.79 | 17 | empty |
| 4 | 59 | 0.31 | 0.76 | 17 | empty |
Compared structures
- 5WNK · Crystal structure of murine receptor-interacting protein 4 (Ripk4) D143N bound to… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ERK0 · AlphaFold monomer V2.0 prediction for receptor-interacting SERINE/THREONINE-protein… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q9ERK0
- Elsewhere: RCSB PDB 5WNK · PDBe 5WNK · UniProt Q9ERK0
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