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Dimeric structure of a hera helicase fragment including the C-terminal reca domain, the dimerization domain, and the RNA binding domain
Analyse Dimeric structure of a hera helicase fragment including the C-terminal reca… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3I32
- Type
- protein
- Length
- 276 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat resistant RNA dependent ATPase
- UniProt
- Q72GF3
- Ligands
- BR
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat resistant RNA dependent ATPase | protein | 276 | 39% helix, 18% strand | Q72GF3 |
Ligands and binding sites
- BR · Bromide ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 529 | 0.68 | 0.78 | 51 | empty |
| 2 | 54 | 0.34 | 0.78 | 12 | empty |
Compared structures
- 3I32 · Dimeric structure of a Hera helicase fragment including the C-terminal RecA domain, the… · 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 Q72GF3
- Elsewhere: RCSB PDB 3I32 · PDBe 3I32 · UniProt Q72GF3
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