Research workbench
Crystal structures of eap domains from staphylococcus aureus reveal an unexpected homology to bacterial superantigens
Analyse Crystal structures of eap domains from staphylococcus aureus reveal an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YN5
- Type
- protein
- Length
- 203 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- EAPH2
- UniProt
- Q99VA9
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | EAPH2 | protein | 103 | 27% helix, 45% strand | Q99VA9 |
| B | EAPH2 | protein | 100 | 25% helix, 44% strand | Q99VA9 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.40 | 0.77 | 15 | empty |
| 2 | 74 | 0.39 | 0.78 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 82 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1YN5 · Crystal Structures of EAP Domains from Staphylococcus aureus Reveal an Unexpected… · 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 Q99VA9
- Elsewhere: RCSB PDB 1YN5 · PDBe 1YN5 · UniProt Q99VA9
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