MolNFT v1 · #161706 · protein
Death-associated protein kinase 1 (DAPK1) catalytic and auto- regulatory domains with S289E and S308A mutations
6QMO: “Death-associated protein kinase 1 (DAPK1) catalytic and auto- regulatory domains with S289E and S308A…”. X-ray diffraction, 1 ligand (CL). MolNFT v1 #161706 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6QMO
- Type
- protein
- Length
- 299 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P53355
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 299 | — | P53355 |
Ligands and binding sites
- CL · Chloride ion · ion · 5 copies · chains A
- GOL · Glycerol · additive · 6 copies · chains A
- PGE · Triethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6QMO · Death-associated Protein Kinase 1 (DAPK1) catalytic and auto-regulatory domains with… · the same entry in another collection · chain A against A, TM-score 1.00
- P53355 · AlphaFold monomer V2.0 prediction for death-associated protein kinase 1 (P53355) · 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 P53355
- Elsewhere: RCSB PDB 6QMO · PDBe 6QMO · UniProt P53355
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