Research workbench
High-resolution X-ray structure of the T26H mutant of T4 lysozyme
Analyse High-resolution X-ray structure of the T26H mutant 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
- 5XPF
- Type
- protein
- Length
- 164 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endolysin
- EC
- 3.2.1.17
- UniProt
- D9IEF7
- Ligands
- NA, CL
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endolysin (EC 3.2.1.17) | protein | 164 | 62% helix, 9% strand | D9IEF7 |
Ligands and binding sites
- NA · Sodium ion · metal · 3 copies · chains A
- CL · Chloride ion · ion · 5 copies · chains A
- HEZ · Hexane-1,6-diol · additive · 4 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.50 | 0.75 | 28 | NA, HEZ |
Compared structures
- 5XPF · High-resolution X-ray structure of the T26H mutant 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 D9IEF7
- Elsewhere: RCSB PDB 5XPF · PDBe 5XPF · UniProt D9IEF7
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