Research workbench
Cell wall binding domain of endolysin from Listeria phage A500.
Analyse Cell wall binding domain of endolysin from Listeria phage A500. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HX0
- Type
- protein
- Length
- 137 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.59
- Source
- Listeria phage A500
- Molecule
- L-alanyl-D-glutamate peptidase
- EC
- 3.4.24.-
- UniProt
- Q37979
Structure
x-ray diffraction · resolution 1.59 · 1 distinct chain · 2% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-alanyl-D-glutamate peptidase (EC 3.4.24.-) | protein | 137 | 2% helix, 47% strand | Q37979 |
Compared structures
- 6HX0 · Cell wall binding domain of endolysin from listeria phage A500. · 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 Q37979
- Elsewhere: RCSB PDB 6HX0 · PDBe 6HX0 · UniProt Q37979
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