Research workbench
Crystal structure of the complex of peptidyl-tRNA hydrolase with N- propanol at 1.43 a resolution
Analyse Crystal structure of the complex of peptidyl-tRNA hydrolase with N- propanol at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IX6
- 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 · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase (EC 3.1.1.29) | protein | 196 | 41% helix, 22% strand | D0C9L6 |
Ligands and binding sites
- POL · N-propanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6IX6 · Crystal structure of the complex of peptidyl-tRNA hydrolase with N-propanol at 1.43 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 6IX6 · PDBe 6IX6 · UniProt D0C9L6
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