MolNFT v1 · #114990 · protein
Crystal structure of prefusion-stabilized rsv F variant sc-tm
5C6B · Fusion glycoprotein F0,FIBRITIN: “Crystal structure of prefusion-stabilized rsv F variant sc-tm”. X-ray diffraction, 2 ligands (SO4, CL), 3 pockets (best druggability 0.44). MolNFT v1 #114990 on GenesisL1: 3D structure, binding…
- PDB
- 5C6B
- Type
- protein
- Length
- 456 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fusion glycoprotein F0,FIBRITIN
- UniProt
- P03420, Q38650
- Ligands
- SO4, CL
- Pockets
- 3 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F | Fusion glycoprotein F0,FIBRITIN | protein | 456 | 30% helix, 32% strand | P03420, Q38650 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains F
- CL · Chloride ion · ion · 2 copies · chains F
- NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · chains F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.44 | 0.77 | 17 | empty |
| 2 | 129 | 0.39 | 0.74 | 23 | empty |
| 3 | 58 | 0.37 | 0.79 | 14 | empty |
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 5C6B · Crystal Structure of Prefusion-stabilized RSV F variant SC-TM · the same entry in another collection · chain F against F, 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 P03420
- Every structure of UniProt Q38650
- Elsewhere: RCSB PDB 5C6B · PDBe 5C6B · UniProt P03420 · UniProt Q38650
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