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Crystal structure of CSN5
Analyse Crystal structure of CSN5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F7O
- Type
- protein
- Length
- 470 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- COP9 signalosome complex subunit 5
- EC
- 3.4.-.-
- UniProt
- Q92905
- Ligands
- ZN, SCN
- Pockets
- 7 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | COP9 signalosome complex subunit 5 (EC 3.4.-.-) | protein | 235 | 34% helix, 23% strand | Q92905 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 744 | 0.76 | 0.81 | 90 | SCN |
| 2 | 125 | 0.54 | 0.82 | 28 | empty |
| 3 | 89 | 0.44 | 0.79 | 15 | empty |
| 4 | 67 | 0.41 | 0.80 | 15 | empty |
| 5 | 109 | 0.41 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1122 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 modified (engineered).
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 4F7O · PDBe 4F7O · UniProt Q92905
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