Research workbench
Crystal structure of HP23L/N36
Analyse Crystal structure of HP23L/N36 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YB3
- Type
- protein
- Length
- 176 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Envelope glycoprotein; HP23L
- UniProt
- Q1HMR5
Structure
x-ray diffraction · 3 distinct chains · 90% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, D | Envelope glycoprotein | protein | 36 | 92% helix, 0% strand | Q1HMR5 |
| F | Envelope glycoprotein | protein | 35 | 94% helix, 0% strand | Q1HMR5 |
| H, G, I | HP23L | protein | 23 | 83% helix, 0% strand | — |
Interfaces
9 interfaces between chains.
- D–F · 722 Ų buried · 5 hydrogen bonds · protein-protein
- E–D · 714 Ų buried · 5 hydrogen bonds · protein-protein
- E–F · 671 Ų buried · 5 hydrogen bonds · protein-protein
- E–G · 614 Ų buried · 1 hydrogen bond · protein-protein
- F–H · 608 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5YB3 · Crystal structure of HP23L/N36 · the same entry in another collection · chain E against E, 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 Q1HMR5
- Elsewhere: RCSB PDB 5YB3 · PDBe 5YB3 · UniProt Q1HMR5
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