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
- 1YN3
- Type
- protein
- Length
- 196 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Truncated cell surface protein MAP-W
- UniProt
- Q99QS1
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Truncated cell surface protein MAP-W | protein | 98 | 26% helix, 43% strand | Q99QS1 |
Compared structures
- 1YN3 · 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
- Q99QS1 · AlphaFold monomer V2.0 prediction for protein MAP (Q99QS1) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q99QS1
- Elsewhere: RCSB PDB 1YN3 · PDBe 1YN3 · UniProt Q99QS1
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