MolNFT v1 · #181478 · protein
Structure of SARS-cov-2 NSP16/NSP10 complex in presence of S-adenosyl- L-homocysteine (sah)
7LW4: “Structure of SARS-cov-2 NSP16/NSP10 complex in presence of S-adenosyl- L-homocysteine (sah)”. X-ray diffraction, 1 ligand (ZN). MolNFT v1 #181478 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7LW4
- Type
- protein
- Length
- 413 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTD1
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 299 | — | P0DTD1 |
| B | — | protein | 114 | — | P0DTD1 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B
- ACT · Acetate ion · additive · 9 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7LW4 · Structure of SARS-CoV-2 nsp16/nsp10 complex in presence of S-adenosyl-L-homocysteine (SAH) · 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 P0DTD1
- Elsewhere: RCSB PDB 7LW4 · PDBe 7LW4 · UniProt P0DTD1
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