Research workbench
Crystal structure of the uvsw helicase from bacteriophage T4
Analyse Crystal structure of the uvsw helicase from bacteriophage T4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RIF
- Type
- protein
- Length
- 564 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA helicase uvsw
- UniProt
- P20703
- Ligands
- AU, MG
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | DNA helicase uvsw | protein | 282 | 40% helix, 21% strand | P20703 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1048 | 0.77 | 0.79 | 77 | empty |
| 2 | 104 | 0.49 | 0.81 | 20 | AU |
| 3 | 73 | 0.46 | 0.83 | 14 | empty |
| 4 | 76 | 0.37 | 0.77 | 16 | empty |
| 5 | 56 | 0.33 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 542 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1RIF · Crystal structure of the UvsW helicase from Bacteriophage T4 · 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 P20703
- Elsewhere: RCSB PDB 1RIF · PDBe 1RIF · UniProt P20703
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