MolNFT v1 · #153518 · protein
Crystal structure at atomic resolution reveals the catalytic mechanism in peptidyl-tRNA hydrolase from acinetobacter baumannii.
6JGU: “Crystal structure at atomic resolution reveals the catalytic mechanism in peptidyl-tRNA hydrolase from…”. X-ray diffraction. MolNFT v1 #153518 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6JGU
- 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 · 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 |
Compared structures
- 6JGU · Crystal structure at atomic resolution reveals the catalytic mechanism in peptidyl-tRNA… · 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 6JGU · PDBe 6JGU · UniProt D0C9L6
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