Research workbench
Complex structure of CSN2 with IP6
Analyse Complex structure of CSN2 with IP6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6A73
- Type
- protein
- Length
- 580 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- COP9 signalosome complex subunit 2,ENDOLYSIN
- EC
- 3.2.1.17
- UniProt
- P61201, A0A097J809
- Ligands
- IHP, SO4
- Pockets
- 4 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | COP9 signalosome complex subunit 2,ENDOLYSIN (EC 3.2.1.17) | protein | 290 | 72% helix, 5% strand | P61201, A0A097J809 |
Ligands and binding sites
- IHP · Inositol hexakisphosphate · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 262 | 0.54 | 0.76 | 32 | empty |
| 2 | 210 | 0.53 | 0.77 | 28 | empty |
| 3 | 94 | 0.45 | 0.80 | 14 | empty |
| 4 | 91 | 0.40 | 0.78 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 649 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 P61201
- Every structure of UniProt A0A097J809
- Elsewhere: RCSB PDB 6A73 · PDBe 6A73 · UniProt P61201 · UniProt A0A097J809
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