Research workbench
Structure of the chaetomium thermophilum ULP1-like sumo protease catalytic domain
Analyse Structure of the chaetomium thermophilum ULP1-like sumo protease catalytic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DG4
- Type
- protein
- Length
- 253 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ULP1-like sumo protease
- EC
- 3.4.22.68
- UniProt
- G0RZV7
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ULP1-like sumo protease (EC 3.4.22.68) | protein | 253 | 48% helix, 13% strand | G0RZV7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.62 | 0.93 | 18 | empty |
| 2 | 108 | 0.43 | 0.77 | 19 | empty |
| 3 | 51 | 0.29 | 0.76 | 13 | empty |
Compared structures
- 6DG4 · Structure of the Chaetomium thermophilum Ulp1-like SUMO protease catalytic domain · the same entry in another collection · chain A against A, TM-score 1.00
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 G0RZV7
- Elsewhere: RCSB PDB 6DG4 · PDBe 6DG4 · UniProt G0RZV7
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