Research workbench
COPS5(2-257) in complex with a azaindole (compound 4)
Analyse COPS5(2-257) in complex with a azaindole (compound 4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5M5Q
- Type
- protein
- Length
- 219 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- COP9 signalosome complex subunit 5
- EC
- 3.4.-.-
- UniProt
- Q92905
- Ligands
- 7K1, ZN
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | COP9 signalosome complex subunit 5 (EC 3.4.-.-) | protein | 219 | 41% helix, 23% strand | Q92905 |
Ligands and binding sites
- 7K1 · 1-[(3~{R})-3-(1~{H}-benzimidazol-2-yl)morpholin-4-yl]-3-[2-(4-methyl-2-phenyl-phenyl)-1~{H}-pyrrolo[2,3-b]pyridin-3-yl]propan-1-one · ligand · chains A
- ZN · Zinc ion · metal · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 291 | 0.57 | 0.77 | 32 | empty |
| 2 | 211 | 0.49 | 0.75 | 33 | MPD |
| 3 | 50 | 0.34 | 0.79 | 14 | empty |
| 4 | 78 | 0.34 | 0.75 | 13 | 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 Q92905
- Elsewhere: RCSB PDB 5M5Q · PDBe 5M5Q · UniProt Q92905
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.