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
- 1YN4
- Type
- protein
- Length
- 99 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- EAPH1
- UniProt
- Q99S64
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | EAPH1 | protein | 99 | 27% helix, 42% strand | Q99S64 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1YN4 · 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 Q99S64
- Elsewhere: RCSB PDB 1YN4 · PDBe 1YN4 · UniProt Q99S64
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