Research workbench
Structural model of human decay-accelerating factor bound to echovirus 7 from cryo-electron microscopy
Analyse Structural model of human decay-accelerating factor bound to echovirus 7 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1M11
- Type
- protein
- Length
- 1,013 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Decay-accelerating factor; Coat protein VP1; Coat protein VP2; Coat protein VP3
- UniProt
- P08174, Q914E0
- Pockets
- 2 · best druggability 0.32
Structure
electron microscopy · 4 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| R | Decay-accelerating factor | protein | 243 | 0% helix, 0% strand | P08174 |
| 1 | Coat protein VP1 | protein | 278 | 0% helix, 0% strand | Q914E0 |
| 2 | Coat protein VP2 | protein | 254 | 0% helix, 0% strand | Q914E0 |
| 3 | Coat protein VP3 | protein | 238 | 0% helix, 0% strand | Q914E0 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.32 | 0.72 | 29 | empty |
| 2 | 60 | 0.29 | 0.72 | 18 | empty |
Interfaces
3 interfaces between chains.
- 1–3 · 612 Ų buried · 0 hydrogen bonds · protein-protein
- 1–2 · 384 Ų buried · 0 hydrogen bonds · protein-protein
- 2–3 · 236 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1M11 · structural model of human decay-accelerating factor bound to echovirus 7 from… · the same entry in another collection · chain R against R, TM-score 1.00
- P08174 · AlphaFold monomer V2.0 prediction for complement decay-accelerating factor (P08174) · a predicted model of the same protein · chain R against A, TM-score 0.40
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 P08174
- Every structure of UniProt Q914E0
- Elsewhere: RCSB PDB 1M11 · PDBe 1M11 · UniProt P08174 · UniProt Q914E0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.