Research workbench
Crystal structure of UTP30
Analyse Crystal structure of UTP30 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YDU
- Type
- protein
- Length
- 477 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribosome biogenesis protein UTP30
- UniProt
- P36144
- Ligands
- PO4
- Pockets
- 7 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribosome biogenesis protein UTP30 | protein | 233 | 31% helix, 22% strand | P36144 |
| B | Ribosome biogenesis protein UTP30 | protein | 244 | 32% helix, 22% strand | P36144 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 739 | 0.75 | 0.80 | 64 | empty |
| 2 | 275 | 0.63 | 0.81 | 45 | empty |
| 3 | 259 | 0.61 | 0.80 | 42 | empty |
| 4 | 148 | 0.47 | 0.77 | 16 | empty |
| 5 | 74 | 0.33 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1782 Ų buried · 18 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 P36144
- Elsewhere: RCSB PDB 5YDU · PDBe 5YDU · UniProt P36144
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.