Research workbench
Structure of hantavirus envelope glycoprotein gc in postfusion conformation in presence of 300 mm kcl
Analyse Structure of hantavirus envelope glycoprotein gc in postfusion conformation in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LK2
- Type
- protein
- Length
- 374 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Envelopment polyprotein
- UniProt
- P08668
- Ligands
- NAG, FUL, K, NA
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Envelopment polyprotein | protein | 374 | 4% helix, 57% strand | P08668 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- FUL · beta-L-fucopyranose · sugar · chains A
- K · Potassium ion · metal · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 571 | 0.64 | 0.75 | 57 | empty |
| 2 | 173 | 0.46 | 0.75 | 31 | empty |
Modifications
Observed in the structure: 9 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 5LK2 · Structure of hantavirus envelope glycoprotein Gc in postfusion conformation in presence… · 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 P08668
- Elsewhere: RCSB PDB 5LK2 · PDBe 5LK2 · UniProt P08668
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