MolNFT v1 · #37321 · protein
Solution structure of the SARS-coronavirus HR2 domain
2FXP · Spike glycoprotein: “Solution structure of the SARS-coronavirus HR2 domain”. Solution nmr, 2 pockets (best druggability 0.63). MolNFT v1 #37321 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2FXP
- Type
- protein
- Length
- 165 residues
- Chains
- 3
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spike glycoprotein
- UniProt
- P59594
- Pockets
- 2 · best druggability 0.63
Structure
solution nmr · 1 distinct chain · 64% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Spike glycoprotein | protein | 55 | 64% helix, 0% strand | P59594 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.63 | 0.94 | 15 | empty |
| 2 | 90 | 0.47 | 0.81 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1057 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 1052 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 1051 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2FXP · Solution Structure of the SARS-Coronavirus HR2 Domain · the same entry in another collection · chain A against A, TM-score 1.00
- 3SCI · Crystal structure of spike protein receptor-binding domain from a predicted SARS… · a predicted model of the same protein · chain B against E, TM-score 0.21
- 3SCJ · Crystal structure of spike protein receptor-binding domain from a predicted SARS… · a predicted model of the same protein · chain B against E, TM-score 0.21
- 3SCK · Crystal structure of spike protein receptor-binding domain from a predicted SARS… · a predicted model of the same protein · chain A against E, TM-score 0.20
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 P59594
- Elsewhere: RCSB PDB 2FXP · PDBe 2FXP · UniProt P59594
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