Research workbench
Rsv G central conserved region bound to Fab CB017.5
Analyse Rsv G central conserved region bound to Fab CB017.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BLH
- Type
- protein
- Length
- 467 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab CB017.5 light chain; Fab CB017.5 heavy chain; Major surface glycoprotein G
- UniProt
- P27025
- Pockets
- 4 · best druggability 0.55
Structure
x-ray diffraction · 3 distinct chains · 8% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Fab CB017.5 light chain | protein | 211 | 7% helix, 49% strand | — |
| H | Fab CB017.5 heavy chain | protein | 221 | 7% helix, 49% strand | — |
| G | Major surface glycoprotein G | protein | 35 | 26% helix, 11% strand | P27025 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · chains L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 364 | 0.55 | 0.74 | 46 | empty |
| 2 | 79 | 0.39 | 0.78 | 20 | empty |
| 3 | 54 | 0.31 | 0.76 | 15 | empty |
| 4 | 66 | 0.29 | 0.74 | 18 | empty |
Interfaces
3 interfaces between chains.
- L–H · 1716 Ų buried · 10 hydrogen bonds · protein-protein
- H–G · 752 Ų buried · 8 hydrogen bonds · protein-protein
- L–G · 344 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 1 modified (disulfide, cyclization).
Compared structures
- 6BLH · RSV G central conserved region bound to Fab CB017.5 · the same entry in another collection · chain L against L, 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 P27025
- Elsewhere: RCSB PDB 6BLH · PDBe 6BLH · UniProt P27025
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