MolNFT v1 · #126331 · protein
Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths
5LZM: “Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths”. X-ray diffraction, 1 ligand (CL). MolNFT v1 #126331 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5LZM
- Type
- protein
- Length
- 162 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00720
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 162 | — | P00720 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A
- BME · Beta-mercaptoethanol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5LZM · Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high… · 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 5LZM · PDBe 5LZM · UniProt P00720
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