Research workbench
Structure of S. cerevisiae HRR25 1-394 (K38R mutant)
Analyse Structure of S. cerevisiae HRR25 1-394 (K38R mutant) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XHL
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Casein kinase I homolog HRR25
- EC
- 2.7.11.1
- UniProt
- P29295
- Ligands
- CKI, SO4
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Casein kinase I homolog HRR25 (EC 2.7.11.1) | protein | 330 | 42% helix, 12% strand | P29295 |
Ligands and binding sites
- CKI · N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide · ligand · chains A
- SO4 · Sulfate ion · ion · 7 copies · 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 | 162 | 0.51 | 0.78 | 21 | CKI |
| 2 | 76 | 0.32 | 0.75 | 19 | empty |
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 P29295
- Elsewhere: RCSB PDB 4XHL · PDBe 4XHL · UniProt P29295
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