MolNFT v1 · #113862 · protein
Crystal structure of DAPK1 in complex with apigenin.
5AUV · Death-associated protein kinase 1: “Crystal structure of DAPK1 in complex with apigenin.”. X-ray diffraction, 2 ligands (AGI, CL), 2 pockets (best druggability 0.68). MolNFT v1 #113862 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5AUV
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Death-associated protein kinase 1
- EC
- 2.7.11.1
- UniProt
- P53355
- Ligands
- AGI, CL
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Death-associated protein kinase 1 (EC 2.7.11.1) | protein | 275 | 35% helix, 20% strand | P53355 |
Ligands and binding sites
- AGI · 5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one · ligand · chains A
- CL · Chloride ion · ion · 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 | 460 | 0.68 | 0.79 | 48 | AGI, CL |
| 2 | 53 | 0.28 | 0.75 | 15 | empty |
Compared structures
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 P53355
- Elsewhere: RCSB PDB 5AUV · PDBe 5AUV · UniProt P53355
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