Research workbench
Crystal structure of human Fab 14N4 in complex with post-fusion rsv F
Analyse Crystal structure of human Fab 14N4 in complex with post-fusion rsv F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5J3D
- Type
- protein
- Length
- 2,598 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14N4 heavy chain; 14N4 light chain; Fusion glycoprotein F0
- UniProt
- P03420
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 21% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, H | 14N4 heavy chain | protein | 220 | 7% helix, 45% strand | — |
| B, D, L | 14N4 light chain | protein | 215 | 5% helix, 50% strand | — |
| E, G, J | Fusion glycoprotein F0 | protein | 73 | 23% helix, 40% strand | P03420 |
| F, I, K | Fusion glycoprotein F0 | protein | 358 | 40% helix, 28% strand | P03420 |
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 569 | 0.85 | 0.91 | 63 | empty |
| 2 | 498 | 0.71 | 0.81 | 61 | empty |
| 3 | 192 | 0.71 | 0.89 | 28 | empty |
| 4 | 661 | 0.64 | 0.74 | 70 | empty |
| 5 | 188 | 0.64 | 0.84 | 36 | empty |
Interfaces
24 interfaces between chains.
- F–K · 4789 Ų buried · 34 hydrogen bonds · protein-protein
- I–K · 4769 Ų buried · 32 hydrogen bonds · protein-protein
- F–I · 4748 Ų buried · 36 hydrogen bonds · protein-protein
- J–K · 3292 Ų buried · 54 hydrogen bonds · protein-protein
- E–F · 3230 Ų buried · 52 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 36 disulfide (disulfide).
Compared structures
- 5J3D · Crystal structure of human Fab 14N4 in complex with post-fusion RSV F · 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
- Elsewhere: RCSB PDB 5J3D · PDBe 5J3D · UniProt P03420
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