Research workbench
Structure of a peptidyl-tRNA hydrolase (pth) from burkholderia thailandensis
Analyse Structure of a peptidyl-tRNA hydrolase (pth) from burkholderia thailandensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3V2I
- Type
- protein
- Length
- 187 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-tRNA hydrolase
- EC
- 3.1.1.29
- UniProt
- Q2T1B9
- Ligands
- UNL
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase (EC 3.1.1.29) | protein | 187 | 44% helix, 22% strand | Q2T1B9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3V2I · Structure of a Peptidyl-tRNA hydrolase (PTH) from Burkholderia thailandensis · the same entry in another collection · chain A against A, TM-score 1.00
- Q2T1B9 · AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q2T1B9) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q2T1B9
- Elsewhere: RCSB PDB 3V2I · PDBe 3V2I · UniProt Q2T1B9
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