Research workbench
Crystal structure of the amyloid-like iikiik segment from the S. aureus biofilm-associated PSMALPHA4
Analyse Crystal structure of the amyloid-like iikiik segment from the S. aureus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FGR
- Type
- protein
- Length
- 12 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Psm alpha-4
- UniProt
- H9BRQ8
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Psm alpha-4 | protein | 6 | 0% helix, 0% strand | H9BRQ8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- B–A · 182 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6FGR · Crystal Structure of the Amyloid-like IIKIIK Segment from the S. aureus… · the same entry in another collection · chain B against B, 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 H9BRQ8
- Elsewhere: RCSB PDB 6FGR · PDBe 6FGR · UniProt H9BRQ8
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