Research workbench
Native T4 RNase H in the absence of divalent metal ions
Analyse Native T4 RNase H in the absence of divalent metal ions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3H8J
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Enterobacteria phage T4
- Molecule
- Ribonuclease H
- EC
- 3.1.26.4
- UniProt
- P13319
- Ligands
- NA, SO4
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · resolution 1.8 · 1 distinct chain · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease H (EC 3.1.26.4) | protein | 297 | 53% helix, 10% strand | P13319 |
Ligands and binding sites
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 | 545 | 0.74 | 0.82 | 64 | empty |
| 2 | 77 | 0.42 | 0.79 | 20 | empty |
Compared structures
- 3H8J · Native T4 RNase H in the absence of divalent metal ions · 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 P13319
- Elsewhere: RCSB PDB 3H8J · PDBe 3H8J · UniProt P13319
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