Research workbench
Helical reconstruction of zika virus complexed with Fab C10
Analyse Helical reconstruction of zika virus complexed with Fab C10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7C2T
- Type
- protein
- Length
- 1,610 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Envelope protein; M protein; Heavy chain from Fab C10; Light chain from Fab C10
- UniProt
- A0A2D1AHP1, A0A2D1AQS6
- Pockets
- 12 · best druggability 0.59
Structure
electron microscopy · 4 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, N | Envelope protein | protein | 494 | 0% helix, 0% strand | A0A2D1AHP1 |
| E, Q | M protein | protein | 75 | 0% helix, 0% strand | A0A2D1AQS6 |
| K, V | Heavy chain from Fab C10 | protein | 127 | 0% helix, 0% strand | — |
| L, W | Light chain from Fab C10 | protein | 109 | 0% helix, 0% strand | — |
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 371 | 0.59 | 0.74 | 60 | empty |
| 2 | 287 | 0.57 | 0.75 | 62 | empty |
| 3 | 348 | 0.57 | 0.73 | 62 | empty |
| 4 | 274 | 0.56 | 0.75 | 69 | empty |
| 5 | 206 | 0.48 | 0.73 | 48 | empty |
Interfaces
16 interfaces between chains.
- N–Q · 282 Ų buried · 0 hydrogen bonds · protein-protein
- B–E · 279 Ų buried · 0 hydrogen bonds · protein-protein
- B–N · 275 Ų buried · 0 hydrogen bonds · protein-protein
- K–L · 147 Ų buried · 0 hydrogen bonds · protein-protein
- V–W · 145 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7C2T · Helical reconstruction of Zika virus complexed with Fab C10 · the same entry in another collection · chain W against W, 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 A0A2D1AHP1
- Every structure of UniProt A0A2D1AQS6
- Elsewhere: RCSB PDB 7C2T · PDBe 7C2T · UniProt A0A2D1AHP1 · UniProt A0A2D1AQS6
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