Research workbench
Structure of thermus thermophilus CSE3 bound to an RNA representing a product complex
Analyse Structure of thermus thermophilus CSE3 bound to an RNA representing a product… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QRR
- Type
- protein + RNA
- Length
- 222 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein TTHB192; RNA (5'…
- UniProt
- Q53WG9
- Pockets
- 3 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative uncharacterized protein TTHB192 | protein | 204 | 27% helix, 37% strand | Q53WG9 |
| B | RNA (5'- R(*GP*UP*CP*CP*CP*CP*AP*CP*GP*CP*GP*UP*GP*UP*GP*GP*GP*(23G))-3') | rna | 18 | — | — |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.46 | 0.80 | 22 | empty |
| 2 | 107 | 0.37 | 0.75 | 19 | empty |
| 3 | 99 | 0.36 | 0.74 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 524 Ų buried · 17 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 1 modified (nucleotide modification).
Compared structures
- 3QRR · Structure of Thermus Thermophilus Cse3 bound to an RNA representing a product complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q53WG9 · AlphaFold monomer V2.0 prediction for CRISPR-associated endoribonuclease CSE3 (Q53WG9) · 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 Q53WG9
- Elsewhere: RCSB PDB 3QRR · PDBe 3QRR · UniProt Q53WG9
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