Research workbench
Structure of UP1 protein
Analyse Structure of UP1 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IVO
- Type
- protein
- Length
- 1,300 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- UP1
- UniProt
- Q9UXT7
- Ligands
- WO4
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | UP1 | protein | 325 | 48% helix, 20% strand | Q9UXT7 |
Ligands and binding sites
- WO4 · Tungstate(vi)ion · ion · 11 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1150 | 0.79 | 0.81 | 95 | empty |
| 2 | 671 | 0.71 | 0.79 | 62 | empty |
| 3 | 638 | 0.71 | 0.79 | 58 | empty |
| 4 | 630 | 0.68 | 0.77 | 57 | empty |
| 5 | 91 | 0.37 | 0.76 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–B · 787 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 660 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 522 Ų buried · 6 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 Q9UXT7
- Elsewhere: RCSB PDB 2IVO · PDBe 2IVO · UniProt Q9UXT7
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