MolNFT v2 · #224560 · protein

Cryo-EM structure of prefusion-stabilized RSV F (DS-Cav1 sc9-10 strain: B18537) in complex with humanized nAb 5B11

8WZ5 · RSV Fusion glycoprotein: “Cryo-EM structure of prefusion-stabilized RSV F (DS-Cav1 sc9-10 strain: B18537) in complex with humanized nAb…”. Electron microscopy at 3.51, 20 pockets (best druggability 0.68). MolNFT v2 #224560 on…

PDB: 8WZ5
Type: protein
Length: 2,013 residues
Chains: 9
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.51
Source: Human respiratory syncytial virus B; Mus musculus
Molecule: RSV Fusion glycoprotein; 5B11 Fab Heavy Chain; 5B11 Fab Light Chain
Pockets: 20 · best druggability 0.68

Structure

electron microscopy · resolution 3.51 · 3 distinct chains · 22% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	RSV Fusion glycoprotein	protein	448	31% helix, 25% strand	—
H, D, E	5B11 Fab Heavy Chain	protein	116	5% helix, 51% strand	—
L, F, G	5B11 Fab Light Chain	protein	107	0% helix, 44% strand	—

Pockets

20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	217	0.68	0.86	24	empty
2	202	0.67	0.85	26	empty
3	150	0.63	0.85	22	empty
4	360	0.60	0.77	24	empty
5	73	0.53	0.86	17	empty

Interfaces

12 interfaces between chains.

B–C · 1181 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 1179 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 1176 Å² buried · 4 hydrogen bonds · protein-protein
H–L · 769 Å² buried · 4 hydrogen bonds · protein-protein
D–F · 769 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 33 disulfide (disulfide).

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 8WZ5 · PDBe 8WZ5

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