Research workbench
Crystal structure of soluble lytic transglycosylase CJ0843 of campylobacter jejuni in complex with bulgecin a
Analyse Crystal structure of soluble lytic transglycosylase CJ0843 of campylobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CFC
- Type
- protein
- Length
- 506 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1L7J388
- Ligands
- BLG, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 506 | — | A0A1L7J388 |
Ligands and binding sites
- BLG · 4-O-(4-O-sulfonyl-N-acetylglucosamininyl)-5-methylhydroxy-L-proline-taurine · ligand · chains A
- SO4 · Sulfate ion · ion · 9 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 A0A1L7J388
- Elsewhere: RCSB PDB 6CFC · PDBe 6CFC · UniProt A0A1L7J388
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