Research workbench
Crystal structure of extracellular domain 1 (ECD1) of ftsx from S. pneumonie in complex with dodecane-trimethylamine
Analyse Crystal structure of extracellular domain 1 (ECD1) of ftsx from S. pneumonie in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HE6
- Type
- protein
- Length
- 234 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0I6INF5
- Ligands
- CAT
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 117 | — | A0A0I6INF5 |
Ligands and binding sites
- CAT · Dodecane-trimethylamine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6HE6 · Crystal structure of Extracellular Domain 1 (ECD1) of FtsX from S. pneumonie in complex… · 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 A0A0I6INF5
- Elsewhere: RCSB PDB 6HE6 · PDBe 6HE6 · UniProt A0A0I6INF5
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