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Crystal structure of the zufsp family member MUG105
Analyse Crystal structure of the zufsp family member MUG105 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OIY
- Type
- protein
- Length
- 488 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin carboxyl-terminal hydrolase MUG105
- EC
- 3.4.19.12
- UniProt
- O13979
- Ligands
- NA
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ubiquitin carboxyl-terminal hydrolase MUG105 (EC 3.4.19.12) | protein | 244 | 37% helix, 20% strand | O13979 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 279 | 0.64 | 0.81 | 29 | empty |
| 2 | 215 | 0.54 | 0.77 | 22 | empty |
| 3 | 125 | 0.40 | 0.75 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 799 Ų buried · 9 hydrogen bonds · protein-protein
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 O13979
- Elsewhere: RCSB PDB 7OIY · PDBe 7OIY · UniProt O13979
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