MolNFT v1 · #140770 · protein
Crystal structure of a dimeric peptidyl-tRNA hydrolase from acinetobacter baumannii at 1.67 a resolution
5YLA: “Crystal structure of a dimeric peptidyl-tRNA hydrolase from acinetobacter baumannii at 1.67 a resolution”. X-ray diffraction, 3 pockets (best druggability 0.47). MolNFT v1 #140770 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5YLA
- 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 0.47
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 | 105 | 0.47 | 0.80 | 24 | empty |
| 2 | 88 | 0.43 | 0.79 | 23 | empty |
| 3 | 52 | 0.27 | 0.74 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 623 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 5YLA · Crystal structure of a dimeric peptidyl-tRNA hydrolase from Acinetobacter baumannii at… · 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 5YLA · PDBe 5YLA · UniProt D0C9L6
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