MolNFT v1 · #172527 · protein
Schmallenberg virus envelope glycoprotein gc fusion domains in postfusion conformation
7A56 · Envelopment polyprotein: “Schmallenberg virus envelope glycoprotein gc fusion domains in postfusion conformation”. X-ray diffraction, 4 ligands (NA, K, CL), 3 pockets (best druggability 0.60). MolNFT v1 #172527 on GenesisL1: 3D…
- PDB
- 7A56
- Type
- protein
- Length
- 419 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Envelopment polyprotein
- UniProt
- H2AM12
- Ligands
- NA, K, CL, PO4
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Envelopment polyprotein | protein | 419 | 5% helix, 53% strand | H2AM12 |
Ligands and binding sites
- NA · Sodium ion · metal · 4 copies · chains A
- K · Potassium ion · metal · chains A
- CL · Chloride ion · ion · 6 copies · chains A
- PO4 · Phosphate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 292 | 0.60 | 0.79 | 38 | CL |
| 2 | 50 | 0.30 | 0.76 | 15 | empty |
| 3 | 57 | 0.29 | 0.75 | 15 | empty |
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 7A56 · Schmallenberg Virus Envelope Glycoprotein Gc Fusion Domains in Postfusion Conformation · 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 H2AM12
- Elsewhere: RCSB PDB 7A56 · PDBe 7A56 · UniProt H2AM12
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