Research workbench
Crystal structure of K37-acetylated SUMO1 in complex with phosphorylated PML-SIM
Analyse Crystal structure of K37-acetylated SUMO1 in complex with phosphorylated PML-SIM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UYS
- Type
- protein
- Length
- 174 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.59
- Source
- Homo sapiens
- Molecule
- Small ubiquitin-related modifier 1; Protein PML
- UniProt
- P63165
Structure
x-ray diffraction · resolution 1.59 · 4 distinct chains · 21% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Small ubiquitin-related modifier 1 | protein | 75 | 24% helix, 36% strand | P63165 |
| B | Protein PML | protein | 12 | 0% helix, 25% strand | — |
| C | Small ubiquitin-related modifier 1 | protein | 76 | 24% helix, 36% strand | P63165 |
| D | Protein PML | protein | 11 | 0% helix, 27% strand | — |
Interfaces
4 interfaces between chains.
- A–B · 647 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 633 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 334 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 220 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (phosphorylation, acetylation).
Compared structures
- 6UYS · Crystal structure of K37-acetylated SUMO1 in complex with phosphorylated pml-sim · 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 0.97
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 6UYS · PDBe 6UYS · UniProt P63165
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