Research workbench
Structure of bat coronavirus RATG13 spike receptor-binding domain complexed with its receptor equine ACE2
Analyse Structure of bat coronavirus RATG13 spike receptor-binding domain complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7W6R
- Type
- protein
- Length
- 792 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Angiotensin-converting enzyme; Spike glycoprotein
- EC
- 3.4.-.-
- UniProt
- F6V9L3, A0A6B9WHD3
- Ligands
- NAG, ZN
- Pockets
- 6 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Angiotensin-converting enzyme (EC 3.4.-.-) | protein | 596 | 64% helix, 5% strand | F6V9L3 |
| B | Spike glycoprotein | protein | 196 | 17% helix, 29% strand | A0A6B9WHD3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 433 | 0.70 | 0.81 | 44 | empty |
| 2 | 364 | 0.66 | 0.80 | 43 | empty |
| 3 | 312 | 0.63 | 0.80 | 31 | empty |
| 4 | 103 | 0.35 | 0.74 | 19 | empty |
| 5 | 58 | 0.32 | 0.76 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 854 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 7W6R · Structure of Bat coronavirus RaTG13 spike receptor-binding domain complexed with its… · the same entry in another collection · chain A against A, 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 F6V9L3
- Every structure of UniProt A0A6B9WHD3
- Elsewhere: RCSB PDB 7W6R · PDBe 7W6R · UniProt F6V9L3 · UniProt A0A6B9WHD3
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