Research workbench
Crystal structure of human CAMK4 in complex with 4-AMINO(SULFAMOYL- phenylamino)-triazole-carbothioic acid (2,6-difluoro-phenyl)-amide)
Analyse Crystal structure of human CAMK4 in complex with 4-AMINO(SULFAMOYL… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W4O
- Type
- protein
- Length
- 278 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CALCIUM/CALMODULIN-dependent protein kinase type IV
- EC
- 2.7.11.17
- UniProt
- Q16566
- Ligands
- DKI
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CALCIUM/CALMODULIN-dependent protein kinase type IV (EC 2.7.11.17) | protein | 278 | 40% helix, 17% strand | Q16566 |
Ligands and binding sites
- DKI · 5-amino-3-{[4-(aminosulfonyl)phenyl]amino}-N-(2,6-difluorophenyl)-1H-1,2,4-triazole-1-carbothioamide · ligand · 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 | 755 | 0.72 | 0.78 | 70 | DKI |
| 2 | 58 | 0.35 | 0.78 | 14 | empty |
Compared structures
- 2W4O · Crystal structure of Human CAMK4 in complex with 4-Amino(sulfamoyl… · the same entry in another collection · chain A against A, TM-score 1.00
- Q16566 · AlphaFold monomer V2.0 prediction for CALCIUM/CALMODULIN-dependent protein kinase type IV… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q16566
- Elsewhere: RCSB PDB 2W4O · PDBe 2W4O · UniProt Q16566
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