Research workbench
1.73A X-ray crystal structure of the conserved C-terminal (cct) of human spak
Analyse 1.73A X-ray crystal structure of the conserved C-terminal (cct) of human spak in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7O86
- Type
- protein
- Length
- 191 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- STE20/SPS1-related proline-alanine-rich protein kinase
- EC
- 2.7.11.1
- UniProt
- Q9UEW8
- Ligands
- NA, CA, MG
- Pockets
- 3 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | STE20/SPS1-related proline-alanine-rich protein kinase (EC 2.7.11.1) | protein | 96 | 26% helix, 30% strand | Q9UEW8 |
| B | STE20/SPS1-related proline-alanine-rich protein kinase (EC 2.7.11.1) | protein | 95 | 32% helix, 31% strand | Q9UEW8 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A, B
- CA · Calcium ion · metal · chains B
- MG · Magnesium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 144 | 0.47 | 0.77 | 27 | empty |
| 2 | 140 | 0.40 | 0.74 | 25 | NA |
| 3 | 81 | 0.40 | 0.78 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 577 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 7O86 · 1.73A X-ray crystal structure of the conserved C-terminal (CCT) of human SPAK · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UEW8 · AlphaFold monomer V2.0 prediction for STE20/SPS1-related proline- alanine-rich protein… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q9UEW8
- Elsewhere: RCSB PDB 7O86 · PDBe 7O86 · UniProt Q9UEW8
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