MolNFT v1 · #32477 · protein
Structure-based design of novel CHK1 inhibitors: insights into hydrogen bonding and protein-ligand affinity
2BRM: “Structure-based design of novel CHK1 inhibitors: insights into hydrogen bonding and protein-ligand affinity”. X-ray diffraction. MolNFT v1 #32477 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2BRM
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- 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 | — | protein | 263 | — | O14757 |
Compared structures
- 2BRM · Structure-based Design of Novel Chk1 Inhibitors: Insights into Hydrogen Bonding and… · the same entry in another collection · chain A against A, 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 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 O14757
- Elsewhere: RCSB PDB 2BRM · PDBe 2BRM · UniProt O14757
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