MolNFT v1 · #115078 · protein
Crystal structure of the SARS coronavirus NSP14-NSP10 complex
5C8U · Non-structural protein 10: “Crystal structure of the SARS coronavirus NSP14-NSP10 complex”. X-ray diffraction, 2 ligands (ZN, MG), 16 pockets (best druggability 0.83). MolNFT v1 #115078 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5C8U
- Type
- protein
- Length
- 1,294 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non-structural protein 10; Guanine-N7 methyltransferase
- EC
- 2.1.1.-, 3.1.13.-
- UniProt
- P0C6X7
- Ligands
- ZN, MG
- Pockets
- 16 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Non-structural protein 10 | protein | 133 | 27% helix, 11% strand | P0C6X7 |
| B, D | Guanine-N7 methyltransferase (EC 2.1.1.-, 3.1.13.-) | protein | 514 | 26% helix, 21% strand | P0C6X7 |
Ligands and binding sites
- ZN · Zinc ion · metal · 10 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1018 | 0.83 | 0.84 | 71 | empty |
| 2 | 548 | 0.74 | 0.81 | 51 | empty |
| 3 | 580 | 0.70 | 0.78 | 54 | empty |
| 4 | 141 | 0.64 | 0.86 | 23 | empty |
| 5 | 151 | 0.56 | 0.81 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2269 Ų buried · 30 hydrogen bonds · protein-protein
- C–D · 2204 Ų buried · 20 hydrogen bonds · protein-protein
- B–D · 772 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 5C8U · Crystal structure of the SARS coronavirus nsp14-nsp10 complex · 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 P0C6X7
- Elsewhere: RCSB PDB 5C8U · PDBe 5C8U · UniProt P0C6X7
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