Research workbench
DCN1 covalently bound to inhibitor 4
Analyse DCN1 covalently bound to inhibitor 4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XOQ
- Type
- protein
- Length
- 357 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme, DCN1-like protein 1 chimera
- EC
- 3.2.1.17
- UniProt
- D9IEF7, Q96GG9
- Ligands
- H9S
- Pockets
- 5 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysozyme, DCN1-like protein 1 chimera (EC 3.2.1.17) | protein | 357 | 63% helix, 7% strand | D9IEF7, Q96GG9 |
Ligands and binding sites
- H9S · (2E)-N-[(2S)-2-cyclohexyl-2-({N-propanoyl-3-[6-(propan-2-yl)-1,3-benzothiazol-2-yl]-L-alanyl}amino)ethyl]-4-(morpholin-4-yl)but-2-enamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 164 | 0.70 | 0.88 | 24 | H9S |
| 2 | 335 | 0.58 | 0.76 | 39 | empty |
| 3 | 85 | 0.35 | 0.75 | 17 | empty |
| 4 | 59 | 0.29 | 0.75 | 15 | empty |
| 5 | 67 | 0.28 | 0.73 | 19 | 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 D9IEF7
- Every structure of UniProt Q96GG9
- Elsewhere: RCSB PDB 6XOQ · PDBe 6XOQ · UniProt D9IEF7 · UniProt Q96GG9
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