Research workbench
Crystal structure of a dimeric inhibited of peptidyl tRNA hydrolase at 1.76A resolution
Analyse Crystal structure of a dimeric inhibited of peptidyl tRNA hydrolase at 1.76A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LSO
- Type
- protein
- Length
- 386 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-tRNA hydrolase
- EC
- 3.1.1.29
- UniProt
- D0C9L6
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Peptidyl-tRNA hydrolase (EC 3.1.1.29) | protein | 193 | 41% helix, 22% strand | D0C9L6 |
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 | 101 | 0.50 | 0.82 | 26 | empty |
| 2 | 120 | 0.49 | 0.80 | 25 | empty |
| 3 | 55 | 0.29 | 0.75 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 553 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 6LSO · Crystal structure of a dimeric inhibited of peptidyl tRNA hydrolase at 1.76A resolution · 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 D0C9L6
- Elsewhere: RCSB PDB 6LSO · PDBe 6LSO · UniProt D0C9L6
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