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The N-terminal domain of pa endonuclease from the influenza H1N1 virus in complex with 3-hydroxy-6-(2-methyl-4-(1H-tetrazol-5-YL)PHENYL)-4- oxo-1,4-dihydropyridine-2-carboxylic acid
Analyse The N-terminal domain of pa endonuclease from the influenza H1N1 virus in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E6W
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- C3W5S0
- Ligands
- HWJ, MN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 174 | — | C3W5S0 |
Ligands and binding sites
- HWJ · 3-hydroxy-6-[2-methyl-4-(1H-tetrazol-5-yl)phenyl]-4-oxo-1,4-dihydropyridine-2-carboxylic acid · ligand · chains A
- MN · Manganese (II) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6E6W · The N-terminal domain of PA endonuclease from the influenza H1N1 virus in complex with… · 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 C3W5S0
- Elsewhere: RCSB PDB 6E6W · PDBe 6E6W · UniProt C3W5S0
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