Research workbench
Crystal structure of peptidyl-tRNA hydrolase from acinetobacter baumannii with 12% peg 1500 at 1.55 a resolution.
Analyse Crystal structure of peptidyl-tRNA hydrolase from acinetobacter baumannii with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IYE
- Type
- protein
- Length
- 196 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
- D0C9L6
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase (EC 3.1.1.29) | protein | 196 | 39% helix, 22% strand | D0C9L6 |
Compared structures
- 6IYE · Crystal structure of peptidyl-tRNA hydrolase from Acinetobacter baumannii with 12% PEG… · 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 6IYE · PDBe 6IYE · UniProt D0C9L6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.