MolNFT v2 · #159564 · protein
SARS-Coronavirus NSP12 bound to NSP7 and NSP8 co-factors
6NUR: “SARS-Coronavirus NSP12 bound to NSP7 and NSP8 co-factors”. Electron microscopy at 3.1, 1 ligand (ZN). MolNFT v2 #159564 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6NUR
- Type
- protein
- Length
- 1,087 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.1
- Source
- Human SARS coronavirus
- UniProt
- P0C6X7, P0C6U8
- Ligands
- ZN
Structure
electron microscopy · resolution 3.1 · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 793 | — | P0C6X7 |
| B | — | protein | 115 | — | P0C6U8 |
| C | — | protein | 70 | — | P0C6X7 |
| D | — | protein | 109 | — | P0C6U8 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6NUR · SARS-coronavirus NSP12 bound to NSP7 and NSP8 co-factors · 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
- Every structure of UniProt P0C6U8
- Elsewhere: RCSB PDB 6NUR · PDBe 6NUR · UniProt P0C6X7 · UniProt P0C6U8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.