MolNFT v1 · #163383 · protein
Structure of the kinase domain of human RIPK2 in complex with the inhibitor CSLP3
6S1F: “Structure of the kinase domain of human RIPK2 in complex with the inhibitor CSLP3”. X-ray diffraction, 1 ligand (KRE). MolNFT v1 #163383 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6S1F
- Type
- protein
- Length
- 1,154 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O43353
- Ligands
- KRE
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 291 | — | O43353 |
| B | — | protein | 286 | — | O43353 |
| C | — | protein | 289 | — | O43353 |
| D | — | protein | 288 | — | O43353 |
Ligands and binding sites
- KRE · ~{N}-[3-[2-azanyl-5-(4-piperazin-1-ylphenyl)pyridin-3-yl]-5-methoxy-phenyl]methanesulfonamide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6S1F · Structure of the kinase domain of human RIPK2 in complex with the inhibitor CSLP3 · the same entry in another collection · chain A against A, TM-score 1.00
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 O43353
- Elsewhere: RCSB PDB 6S1F · PDBe 6S1F · UniProt O43353
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