Research workbench
Crystal structure of A.FULGIDUS RIO2 kinase complexed with ATP and manganese ions
Analyse Crystal structure of A.FULGIDUS RIO2 kinase complexed with ATP and manganese… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZAO
- Type
- protein
- Length
- 271 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RIO2 serine kinase
- UniProt
- O30245
- Ligands
- ATP, MN, PO4
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RIO2 serine kinase | protein | 271 | 44% helix, 21% strand | O30245 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MN · Manganese (II) ion · metal · 2 copies · chains A
- PO4 · Phosphate ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 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 | 291 | 0.62 | 0.79 | 29 | MN, PO4, ATP |
| 2 | 69 | 0.34 | 0.76 | 18 | empty |
Compared structures
- 1ZAO · Crystal Structure of A.fulgidus Rio2 Kinase Complexed With ATP and Manganese Ions · the same entry in another collection · chain A against A, TM-score 1.00
- O30245 · AlphaFold monomer V2.0 prediction for rio-type SERINE/THREONINE- protein kinase RIO2… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O30245
- Elsewhere: RCSB PDB 1ZAO · PDBe 1ZAO · UniProt O30245
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