MolNFT v1 · #12676 · protein
X-ray structure of the hpr KINASE/PHOSPHATASE from staphylococcus xylosus at 1.95 a resolution
1KO7: “X-ray structure of the hpr KINASE/PHOSPHATASE from staphylococcus xylosus at 1.95 a resolution”. X-ray diffraction, 1 ligand (PO4), 6 pockets (best druggability 0.65). MolNFT v1 #12676 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1KO7
- Type
- protein
- Length
- 570 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hpr KINASE/PHOSPHATASE
- EC
- 2.7.1.-, 3.1.3.-
- UniProt
- Q9S1H5
- Ligands
- PO4
- Pockets
- 6 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hpr KINASE/PHOSPHATASE (EC 2.7.1.-, 3.1.3.-) | protein | 285 | 36% helix, 29% strand | Q9S1H5 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 603 | 0.65 | 0.75 | 62 | empty |
| 2 | 110 | 0.64 | 0.89 | 35 | empty |
| 3 | 189 | 0.45 | 0.74 | 25 | empty |
| 4 | 56 | 0.32 | 0.77 | 15 | PO4 |
| 5 | 55 | 0.26 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1462 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 1KO7 · X-ray structure of the HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9S1H5 · AlphaFold monomer V2.0 prediction for hpr KINASE/PHOSPHORYLASE (Q9S1H5) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q9S1H5
- Elsewhere: RCSB PDB 1KO7 · PDBe 1KO7 · UniProt Q9S1H5
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