MolNFT v1 · #35389 · protein
Structure of H-CHK1 complexed with A859017
2E9V: “Structure of H-CHK1 complexed with A859017”. X-ray diffraction. MolNFT v1 #35389 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2E9V
- Type
- protein
- Length
- 536 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O14757
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 268 | — | O14757 |
Compared structures
- 2E9V · Structure of h-CHK1 complexed with A859017 · the same entry in another collection · chain B against B, TM-score 1.00
- O14757 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase CHK1 (O14757) · a predicted model of the same protein · chain B against A, TM-score 0.96
- 2C3K · Identification of a buried pocket for potent and selective inhibition of CHK1: prediction… · a predicted model of the same protein · chain A against A, TM-score 0.96
- 2C3L · Identification of a buried pocket for potent and selective inhibition of CHK1: prediction… · a predicted model of the same protein · chain B against A, TM-score 0.96
- 2C3J · Identification of a buried pocket for potent and selective inhibition of CHK1: prediction… · a predicted model of the same protein · chain B against A, TM-score 0.94
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 O14757
- Elsewhere: RCSB PDB 2E9V · PDBe 2E9V · UniProt O14757
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