MolNFT v1 · #52670 · protein
Structure of the PDZ domain of human microtubule associated serine-threonine kinase 4
2W7R · Microtubule-associated SERINE/THREONINE-protein kinase 4: “Structure of the PDZ domain of human microtubule associated serine-threonine kinase 4”. X-ray diffraction, 1 ligand (PO4), 7 pockets (best druggability 0.35). MolNFT v1…
- PDB
- 2W7R
- Type
- protein
- Length
- 190 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Microtubule-associated SERINE/THREONINE-protein kinase 4
- EC
- 2.7.11.1
- UniProt
- O15021
- Ligands
- PO4
- Pockets
- 7 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Microtubule-associated SERINE/THREONINE-protein kinase 4 (EC 2.7.11.1) | protein | 95 | 15% helix, 39% strand | O15021 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.35 | 0.77 | 17 | PO4 |
| 2 | 61 | 0.35 | 0.77 | 15 | empty |
| 3 | 74 | 0.31 | 0.74 | 16 | empty |
| 4 | 63 | 0.31 | 0.75 | 18 | empty |
| 5 | 55 | 0.29 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1087 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 2W7R · Structure of the PDZ domain of Human Microtubule associated serine- threonine kinase 4 · the same entry in another collection · chain B against B, TM-score 1.00
- O15021 · AlphaFold monomer V2.0 prediction for microtubule-associated SERINE/THREONINE-protein… · a predicted model of the same protein · chain A against A, TM-score 0.82
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 O15021
- Elsewhere: RCSB PDB 2W7R · PDBe 2W7R · UniProt O15021
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