MolNFT v1 · #100079 · protein
Crystal structure of prefusion-stabilized rsv F variant ds-CAV1 at pH 9.5
4MMT · Fusion glycoprotein F2: “Crystal structure of prefusion-stabilized rsv F variant ds-CAV1 at pH 9.5”. X-ray diffraction, 2 pockets (best druggability 0.62). MolNFT v1 #100079 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4MMT
- Type
- protein
- Length
- 453 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fusion glycoprotein F2; Fusion glycoprotein F1 fused with fibritin trimerization domain
- UniProt
- P03420, P10104
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fusion glycoprotein F2 | protein | 73 | 27% helix, 37% strand | P03420 |
| B | Fusion glycoprotein F1 fused with fibritin trimerization domain | protein | 380 | 30% helix, 31% strand | P03420, P10104 |
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 | 191 | 0.62 | 0.83 | 32 | empty |
| 2 | 50 | 0.28 | 0.75 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 4178 Ų buried · 78 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 4MMT · Crystal Structure of Prefusion-stabilized RSV F Variant DS-Cav1 at pH 9.5 · 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 P03420
- Every structure of UniProt P10104
- Elsewhere: RCSB PDB 4MMT · PDBe 4MMT · UniProt P03420 · UniProt P10104
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