Research workbench
Fphf, staphylococcus aureus fluorophosphonate-binding serine hydrolases F, KT130 bound
Analyse Fphf, staphylococcus aureus fluorophosphonate-binding serine hydrolases F… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VHE
- Type
- protein
- Length
- 1,020 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0D6GS23
- Ligands
- 6WG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 255 | — | A0A0D6GS23 |
Ligands and binding sites
- 6WG · (2~{R})-2-phenylpiperidine-1-carbaldehyde · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VHE · FphF, Staphylococcus aureus fluorophosphonate-binding serine hydrolases F, KT130 bound · 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 A0A0D6GS23
- Elsewhere: RCSB PDB 6VHE · PDBe 6VHE · UniProt A0A0D6GS23
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