MolNFT v1 · #109454 · protein
Crystal structure of the autolysin lyta from streptococcus pneumoniae TIGR4
4X36: “Crystal structure of the autolysin lyta from streptococcus pneumoniae TIGR4”. X-ray diffraction, 2 ligands (CHT, ZN), 1 pocket (best druggability 0.41). MolNFT v1 #109454 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4X36
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Autolysin
- EC
- 3.5.1.28
- UniProt
- P06653
- Ligands
- CHT, ZN
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Autolysin (EC 3.5.1.28) | protein | 318 | 19% helix, 29% strand | P06653 |
Ligands and binding sites
- CHT · Choline ion · ligand · 5 copies · chains A
- ZN · Zinc ion · metal · chains A
- GOL · Glycerol · additive · 6 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 | 129 | 0.41 | 0.75 | 25 | empty |
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
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 P06653
- Elsewhere: RCSB PDB 4X36 · PDBe 4X36 · UniProt P06653
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