Research workbench
Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme
Analyse Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 178L
- Type
- protein
- Length
- 162 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T4 lysozyme
- EC
- 3.2.1.17
- UniProt
- P00720
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T4 lysozyme (EC 3.2.1.17) | protein | 162 | 64% helix, 9% strand | P00720 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 178L · Protein flexibility and adaptability seen in 25 crystal forms of T4 LYSOZYME · 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 178L · PDBe 178L · UniProt P00720
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