Research workbench
Coxsackievirus A21 capsid subdomain in complex with mouse polyclonal antibody pAbC-5
Analyse Coxsackievirus A21 capsid subdomain in complex with mouse polyclonal antibody… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TQT
- Type
- protein
- Length
- 4,418 residues
- Chains
- 22
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 4.1
- Source
- Coxsackievirus A21; Mus musculus
- Molecule
- pAbC-5 light chain; pAbC-5 heavy chain; VP1; VP2; VP3; VP4
- EC
- 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48
- UniProt
- Q7T7N6
- Ligands
- MYR
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · resolution 4.1 · 17 distinct chains · 11% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | pAbC-5 light chain | protein | 98 | 0% helix, 34% strand | — |
| H | pAbC-5 heavy chain | protein | 108 | 0% helix, 33% strand | — |
| a | VP1 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 281 | 13% helix, 31% strand | Q7T7N6 |
| b | VP2 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 264 | 16% helix, 36% strand | Q7T7N6 |
| c | VP3 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 239 | 8% helix, 35% strand | Q7T7N6 |
| d, h, l, t | VP4 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 68 | 10% helix, 18% strand | Q7T7N6 |
| e | VP1 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 282 | 11% helix, 31% strand | Q7T7N6 |
| f | VP2 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 258 | 12% helix, 40% strand | Q7T7N6 |
| g, o | VP3 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 234 | 10% helix, 31% strand | Q7T7N6 |
| i, q | VP1 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 283 | 11% helix, 30% strand | Q7T7N6 |
| j | VP2 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 257 | 11% helix, 38% strand | Q7T7N6 |
| k | VP3 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 233 | 9% helix, 35% strand | Q7T7N6 |
| m | VP1 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 276 | 12% helix, 30% strand | Q7T7N6 |
| n | VP2 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 261 | 11% helix, 37% strand | Q7T7N6 |
| p | VP4 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 67 | 10% helix, 16% strand | Q7T7N6 |
| r | VP2 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 253 | 13% helix, 36% strand | Q7T7N6 |
| s | VP3 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 235 | 9% helix, 34% strand | Q7T7N6 |
Ligands and binding sites
- MYR · Myristic acid · ligand · 5 copies · chains a, c, e, g, i, m, q, s
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 374 | 0.87 | 0.95 | 56 | MYR |
| 2 | 605 | 0.86 | 0.90 | 98 | MYR |
| 3 | 948 | 0.86 | 0.87 | 84 | empty |
| 4 | 344 | 0.86 | 0.94 | 56 | MYR |
| 5 | 427 | 0.85 | 0.92 | 74 | MYR |
Interfaces
102 interfaces between chains.
- a–c · 4239 Ų buried · 56 hydrogen bonds · protein-protein
- m–o · 3912 Ų buried · 58 hydrogen bonds · protein-protein
- e–g · 3907 Ų buried · 56 hydrogen bonds · protein-protein
- i–k · 3898 Ų buried · 60 hydrogen bonds · protein-protein
- q–s · 3838 Ų buried · 50 hydrogen bonds · protein-protein
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 Q7T7N6
- Elsewhere: RCSB PDB 7TQT · PDBe 7TQT · UniProt Q7T7N6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.