Research workbench
Crystal structure of S. cerevisiae sumo E3 ligase SIZ1
Analyse Crystal structure of S. cerevisiae sumo E3 ligase SIZ1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3I2D
- Type
- protein
- Length
- 280 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 sumo-protein ligase SIZ1
- EC
- 6.-.-.-
- UniProt
- Q04195
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 sumo-protein ligase SIZ1 (EC 6.-.-.-) | protein | 280 | 21% helix, 34% strand | Q04195 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.39 | 0.78 | 18 | 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 Q04195
- Elsewhere: RCSB PDB 3I2D · PDBe 3I2D · UniProt Q04195
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