Research workbench
2.1 A crystal structure of Pseudomonas aeruginosa rnase T (Ribonuclease T)
Analyse 2.1 A crystal structure of Pseudomonas aeruginosa rnase T (Ribonuclease T) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F96
- Type
- protein
- Length
- 404 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.09
- Source
- Pseudomonas aeruginosa
- Molecule
- Ribonuclease T
- EC
- 3.1.13.-
- UniProt
- Q9HY82
- Ligands
- MG
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · resolution 2.09 · 1 distinct chain · 41% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ribonuclease T (EC 3.1.13.-) | protein | 202 | 41% helix, 24% strand | Q9HY82 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
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 | 671 | 0.67 | 0.76 | 56 | MG |
| 2 | 284 | 0.57 | 0.77 | 33 | MG |
| 3 | 59 | 0.29 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1354 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 2F96 · 2.1 a crystal structure of pseudomonas aeruginosa RNase T (ribonuclease T) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HY82 · AlphaFold monomer V2.0 prediction for ribonuclease T (Q9HY82) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9HY82
- Elsewhere: RCSB PDB 2F96 · PDBe 2F96 · UniProt Q9HY82
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