Research workbench
Crystal structure of pneumococcal peptidoglycan hydrolase lytb
Analyse Crystal structure of pneumococcal peptidoglycan hydrolase lytb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Q2W
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative endo-beta-N-acetylglucosaminidase
- EC
- 3.2.1.96
- UniProt
- P59205
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative endo-beta-N-acetylglucosaminidase (EC 3.2.1.96) | protein | 263 | 30% helix, 21% strand | P59205 |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 4Q2W · Crystal Structure of pneumococcal peptidoglycan hydrolase LytB · the same entry in another collection · chain A against A, TM-score 1.00
- P59205 · AlphaFold monomer V2.0 prediction for putative endo-beta-N- acetylglucosaminidase (P59205) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P59205
- Elsewhere: RCSB PDB 4Q2W · PDBe 4Q2W · UniProt P59205
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