Research workbench
Engineering domain-swapped binding interfaces by mutually exclusive folding: insertion of ubiquitin into position 103 of barnase
Analyse Engineering domain-swapped binding interfaces by mutually exclusive folding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3Q3F
- Type
- protein
- Length
- 188 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RIBONUCLEASE/UBIQUITIN chimeric protein
- UniProt
- P00648, P0CG48
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RIBONUCLEASE/UBIQUITIN chimeric protein | protein | 188 | 22% helix, 24% strand | P00648, P0CG48 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 16 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 261 | 0.65 | 0.82 | 38 | SO4 |
Compared structures
- 3Q3F · Engineering Domain-Swapped Binding Interfaces by Mutually Exclusive Folding: Insertion of… · the same entry in another collection · chain A against A, TM-score 1.00
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 P00648
- Every structure of UniProt P0CG48
- Elsewhere: RCSB PDB 3Q3F · PDBe 3Q3F · UniProt P00648 · UniProt P0CG48
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