Research workbench
HRV14 in complex with its receptor icam-1
Analyse HRV14 in complex with its receptor icam-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BG7
- Type
- protein
- Length
- 885 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Genome polyprotein; Intercellular adhesion molecule 1
- EC
- 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48
- UniProt
- P03303, P05362
- Pockets
- 13 · best druggability 0.81
Structure
electron microscopy · 5 distinct chains · 9% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | Genome polyprotein (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 274 | 9% helix, 32% strand | P03303 |
| 2 | Genome polyprotein (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 250 | 12% helix, 38% strand | P03303 |
| 3 | Genome polyprotein (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 236 | 7% helix, 31% strand | P03303 |
| 4 | Genome polyprotein (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 41 | 24% helix, 5% strand | P03303 |
| B | Intercellular adhesion molecule 1 | protein | 84 | 0% helix, 45% strand | P05362 |
Pockets
13 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 150 | 0.81 | 0.97 | 26 | empty |
| 2 | 679 | 0.75 | 0.81 | 76 | empty |
| 3 | 156 | 0.46 | 0.76 | 33 | empty |
| 4 | 104 | 0.43 | 0.77 | 26 | empty |
| 5 | 110 | 0.43 | 0.77 | 25 | empty |
Interfaces
9 interfaces between chains.
- 1–3 · 4163 Ų buried · 63 hydrogen bonds · protein-protein
- 1–2 · 2070 Ų buried · 41 hydrogen bonds · protein-protein
- 2–3 · 1625 Ų buried · 19 hydrogen bonds · protein-protein
- 1–B · 945 Ų buried · 10 hydrogen bonds · protein-protein
- 3–4 · 844 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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
- Every structure of UniProt P05362
- Elsewhere: RCSB PDB 7BG7 · PDBe 7BG7 · UniProt P03303 · UniProt P05362
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.