Research workbench
Crystal structure analysis of RNase J
Analyse Crystal structure analysis of RNase J in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BK1
- Type
- protein
- Length
- 551 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metal dependent hydrolase
- EC
- 3.-.-.-
- UniProt
- Q72JJ7
- Ligands
- ZN, SO4
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metal dependent hydrolase (EC 3.-.-.-) | protein | 551 | 34% helix, 26% strand | Q72JJ7 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 565 | 0.74 | 0.82 | 66 | SO4 |
| 2 | 117 | 0.61 | 0.86 | 26 | empty |
| 3 | 159 | 0.46 | 0.76 | 26 | empty |
Modifications
Observed in the structure: 14 modified (engineered).
Compared structures
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 Q72JJ7
- Elsewhere: RCSB PDB 3BK1 · PDBe 3BK1 · UniProt Q72JJ7
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