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Crystal structure of human UTP15
Analyse Crystal structure of human UTP15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RUO
- Type
- protein
- Length
- 601 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- U3 small nucleolar RNA-associated protein 15 homolog
- UniProt
- Q8TED0
- Ligands
- UNX
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | U3 small nucleolar RNA-associated protein 15 homolog | protein | 301 | 3% helix, 51% strand | Q8TED0 |
| B | U3 small nucleolar RNA-associated protein 15 homolog | protein | 300 | 3% helix, 51% strand | Q8TED0 |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 5 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1061 | 0.79 | 0.81 | 95 | empty |
| 2 | 802 | 0.77 | 0.81 | 59 | UNX |
| 3 | 116 | 0.51 | 0.81 | 20 | empty |
| 4 | 128 | 0.40 | 0.74 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 598 Ų buried · 4 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 Q8TED0
- Elsewhere: RCSB PDB 7RUO · PDBe 7RUO · UniProt Q8TED0
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