MolNFT v1 · #137045 · protein
Crystal structure of human WEE1 kinase domain in complex with pd- 166285
5VC5: “Crystal structure of human WEE1 kinase domain in complex with pd- 166285”. X-ray diffraction, 2 ligands (96M, CL). MolNFT v1 #137045 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5VC5
- Type
- protein
- Length
- 261 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P30291
- Ligands
- 96M, CL
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 261 | — | P30291 |
Ligands and binding sites
- 96M · 6-(2,6-dichlorophenyl)-2-({4-[2-(diethylamino) ethoxy]phenyl}amino)-8-methylpyrido[2,3-d]pyrimidin-7(8H)-one · ligand · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5VC5 · Crystal structure of human WEE1 kinase domain in complex with PD-166285 · the same entry in another collection · chain A against A, TM-score 1.00
- P30291 · AlphaFold monomer V2.0 prediction for WEE1-like protein kinase (P30291) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P30291
- Elsewhere: RCSB PDB 5VC5 · PDBe 5VC5 · UniProt P30291
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