MolNFT v1 · #113827 · protein
RIP2 kinase catalytic domain (1 - 310)
5AR2 · Receptor-interacting SERINE/THREONINE-protein kinase 2: “RIP2 kinase catalytic domain (1 - 310)”. X-ray diffraction, 1 ligand (CA), 7 pockets (best druggability 0.83). MolNFT v1 #113827 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5AR2
- Type
- protein
- Length
- 562 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-interacting SERINE/THREONINE-protein kinase 2
- EC
- 2.7.11.1
- UniProt
- O43353
- Ligands
- CA
- Pockets
- 7 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-interacting SERINE/THREONINE-protein kinase 2 (EC 2.7.11.1) | protein | 277 | 39% helix, 16% strand | O43353 |
| B | Receptor-interacting SERINE/THREONINE-protein kinase 2 (EC 2.7.11.1) | protein | 285 | 38% helix, 17% strand | O43353 |
Ligands and binding sites
- CA · Calcium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1075 | 0.83 | 0.84 | 85 | empty |
| 2 | 398 | 0.64 | 0.78 | 44 | empty |
| 3 | 282 | 0.59 | 0.78 | 28 | empty |
| 4 | 134 | 0.48 | 0.78 | 26 | empty |
| 5 | 65 | 0.37 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1881 Ų buried · 21 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 O43353
- Elsewhere: RCSB PDB 5AR2 · PDBe 5AR2 · UniProt O43353
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