MolNFT v1 · #180188 · protein
Structural impact on SARS-cov-2 spike protein by D614G substitution
7KRR: “Structural impact on SARS-cov-2 spike protein by D614G substitution”. Electron microscopy, 3 ligands (NAG, MAN, FUC). MolNFT v1 #180188 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7KRR
- Type
- protein
- Length
- 3,310 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTC2
- Ligands
- NAG, MAN, FUC
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 1091 | — | P0DTC2 |
| C | — | protein | 1110 | — | P0DTC2 |
| A | — | protein | 1109 | — | P0DTC2 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 86 copies · chains B, C, A
- MAN · alpha-D-mannopyranose · sugar · 6 copies
- FUC · alpha-L-fucopyranose · sugar · 3 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7KRR · Structural impact on SARS-CoV-2 spike protein by D614G substitution · the same entry in another collection · chain B against B, 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 P0DTC2
- Elsewhere: RCSB PDB 7KRR · PDBe 7KRR · UniProt P0DTC2
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