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Crystal structure of Peptidyl-tRNA hydrolase from Acinetobacter baumannii at 0.95 A resolution
Analyse Crystal structure of Peptidyl-tRNA hydrolase from Acinetobacter baumannii at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6J93
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 0.95
- Source
- Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / CIP 70.34 / JCM 6841 /…
- Molecule
- Peptidyl-tRNA hydrolase
- EC
- 3.1.1.29
- UniProt
- D0C9L6
Structure
x-ray diffraction · resolution 0.95 · 1 distinct chain · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase (EC 3.1.1.29) | protein | 196 | 40% helix, 21% strand | D0C9L6 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6J93 · Crystal structure of peptidyl-tRNA hydrolase from acinetobacter baumannii at 0.95 a… · 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 6J93 · PDBe 6J93 · UniProt D0C9L6
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