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Crystal structure of extracellular domain 1 (ECD1) of ftsx from S. pneumonie in complex with undecyl-maltoside
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
- 6HEE
- Type
- protein
- Length
- 216 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsx
- UniProt
- Q04LE4
- Ligands
- UMQ, SO4
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsx | protein | 116 | 32% helix, 28% strand | Q04LE4 |
| B | Cell division protein ftsx | protein | 100 | 32% helix, 15% strand | Q04LE4 |
Ligands and binding sites
- UMQ · Undecyl-maltoside · ligand · chains A, B
- SO4 · Sulfate ion · ion · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 187 | 0.53 | 0.78 | 28 | empty |
| 2 | 67 | 0.38 | 0.78 | 12 | UMQ |
| 3 | 51 | 0.29 | 0.75 | 11 | TRS |
Interfaces
1 interface between chains.
- A–B · 890 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6HEE · 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
- Q04LE4 · AlphaFold monomer V2.0 prediction for cell division protein ftsx (Q04LE4) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q04LE4
- Elsewhere: RCSB PDB 6HEE · PDBe 6HEE · UniProt Q04LE4
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