Research workbench
Fab complexed with intact human rhinovirus
Analyse Fab complexed with intact human rhinovirus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RVF
- Type
- protein
- Length
- 1,033 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human rhinovirus 14 coat protein; Fab 17-ia
- UniProt
- P03303
- Pockets
- 18 · best druggability 0.78
Structure
x-ray diffraction · 6 distinct chains · 7% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | Human rhinovirus 14 coat protein | protein | 273 | 8% helix, 29% strand | P03303 |
| 2 | Human rhinovirus 14 coat protein | protein | 255 | 10% helix, 25% strand | P03303 |
| 3 | Human rhinovirus 14 coat protein | protein | 236 | 9% helix, 25% strand | P03303 |
| 4 | Human rhinovirus 14 coat protein | protein | 40 | 10% helix, 3% strand | P03303 |
| L | Fab 17-ia | protein | 110 | 0% helix, 38% strand | — |
| H | Fab 17-ia | protein | 119 | 3% helix, 34% strand | — |
Pockets
18 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.78 | 0.95 | 29 | empty |
| 2 | 792 | 0.71 | 0.77 | 85 | empty |
| 3 | 73 | 0.59 | 0.89 | 21 | empty |
| 4 | 163 | 0.49 | 0.77 | 19 | empty |
| 5 | 127 | 0.46 | 0.78 | 23 | empty |
Interfaces
11 interfaces between chains.
- 1–3 · 4125 Ų buried · 64 hydrogen bonds · protein-protein
- 1–2 · 2085 Ų buried · 35 hydrogen bonds · protein-protein
- 2–3 · 1692 Ų buried · 12 hydrogen bonds · protein-protein
- 1–4 · 921 Ų buried · 13 hydrogen bonds · protein-protein
- 3–4 · 877 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 1RVF · Fab complexed with intact human rhinovirus · the same entry in another collection · chain 1 against 1, 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 P03303
- Elsewhere: RCSB PDB 1RVF · PDBe 1RVF · UniProt P03303
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