Research workbench
Crystal structure of SUMO1 in complex with phosphorylated daxx
Analyse Crystal structure of SUMO1 in complex with phosphorylated daxx in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WJP
- Type
- protein
- Length
- 179 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Small ubiquitin-related modifier 1; Daxx
- UniProt
- P63165
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 4 distinct chains · 20% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Small ubiquitin-related modifier 1 | protein | 79 | 23% helix, 34% strand | P63165 |
| B | Daxx | protein | 11 | 0% helix, 27% strand | — |
| C | Small ubiquitin-related modifier 1 | protein | 77 | 23% helix, 35% strand | P63165 |
| D | Daxx | protein | 12 | 0% helix, 25% strand | — |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 132 | 0.43 | 0.76 | 23 | empty |
Interfaces
4 interfaces between chains.
- C–D · 642 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 590 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 249 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 22 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (phosphorylation).
Compared structures
- 4WJP · Crystal Structure of SUMO1 in complex with phosphorylated Daxx · the same entry in another collection · chain A against A, TM-score 1.00
- P63165 · AlphaFold monomer V2.0 prediction for small ubiquitin-related modifier 1 (P63165) · a predicted model of the same protein · chain C against A, TM-score 0.95
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 P63165
- Elsewhere: RCSB PDB 4WJP · PDBe 4WJP · UniProt P63165
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