MolNFT v1 · #125807 · protein
Structure of hantavirus envelope glycoprotein gc in postfusion conformation in presence of 300 mm kcl
5LK2 · Envelopment polyprotein: “Structure of hantavirus envelope glycoprotein gc in postfusion conformation in presence of 300 mm kcl”. X-ray diffraction, 4 ligands (NAG, FUL, K), 2 pockets (best druggability 0.64). MolNFT v1 #125807 on…
- 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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