Research workbench
Crystal structure of A.FULGIDUS RIO1 serine protein kinase
Analyse Crystal structure of A.FULGIDUS RIO1 serine protein kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZTF
- Type
- protein
- Length
- 253 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RIO1 serine protein kinase
- Ligands
- XYA
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RIO1 serine protein kinase | protein | 253 | 43% helix, 23% strand | — |
Ligands and binding sites
- XYA · 2-(6-amino-octahydro-purin-9-yl)-5-hydroxymethyl-tetrahydro-furan-3,4-diol · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 283 | 0.62 | 0.80 | 29 | XYA |
| 2 | 63 | 0.35 | 0.77 | 13 | empty |
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 1ZTF · Crystal Structure of A.fulgidus Rio1 serine protein kinase · 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
- Elsewhere: RCSB PDB 1ZTF · PDBe 1ZTF
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