MolNFT v2 · #13274 · protein
Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme
1L62: “Analysis of the interaction between charged side chains and the alpha-helix dipole using designed…”. X-ray diffraction at 1.7. MolNFT v2 #13274 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1L62
- Type
- protein
- Length
- 162 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.7
- Source
- Enterobacteria phage T4
- UniProt
- P00720
Structure
x-ray diffraction · resolution 1.7 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 162 | — | P00720 |
Compared structures
- 1L62 · Analysis of the interaction between charged side chains and the alpha- helix dipole using… · 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 P00720
- Elsewhere: RCSB PDB 1L62 · PDBe 1L62 · UniProt P00720
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