Research workbench
Structure-based discovery of a novel small-molecule inhibitor of methicillin-resistant S. aureus
Analyse Structure-based discovery of a novel small-molecule inhibitor of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6U3T
- Type
- protein
- Length
- 504 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P09616
- Ligands
- PQJ, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 251 | — | P09616 |
| B | — | protein | 253 | — | P09616 |
Ligands and binding sites
- PQJ · fos-choline-14 · ligand · 4 copies · chains A, B
- SO4 · Sulfate ion · ion · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6U3T · Structure-based discovery of a novel small-molecule inhibitor of methicillin-resistant S.… · the same entry in another collection · chain A against A, TM-score 1.00
- P09616 · AlphaFold monomer V2.0 prediction for alpha-hemolysin (P09616) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P09616
- Elsewhere: RCSB PDB 6U3T · PDBe 6U3T · UniProt P09616
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