MolNFT v1 · #140812 · protein
Crystal structure of MERS-cov NSP16/NSP10 complex bound to sah
5YN8 · NSP16 protein: “Crystal structure of MERS-cov NSP16/NSP10 complex bound to sah”. X-ray diffraction, 2 ligands (SAH, ZN), 2 pockets (best druggability 0.46). MolNFT v1 #140812 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5YN8
- Type
- protein
- Length
- 398 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NSP16 protein; NSP10 protein
- UniProt
- K0BWD0, K4LC41
- Ligands
- SAH, ZN
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NSP16 protein | protein | 281 | 28% helix, 23% strand | K0BWD0 |
| B | NSP10 protein | protein | 117 | 26% helix, 13% strand | K4LC41 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 118 | 0.46 | 0.78 | 19 | empty |
| 2 | 115 | 0.42 | 0.77 | 27 | SAH |
Interfaces
1 interface between chains.
- A–B · 997 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5YN8 · Crystal structure of MERS-CoV nsp16/nsp10 complex bound to SAH · 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 K0BWD0
- Every structure of UniProt K4LC41
- Elsewhere: RCSB PDB 5YN8 · PDBe 5YN8 · UniProt K0BWD0 · UniProt K4LC41
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