Research workbench
The hantavirus glycoprotein G1 tail contains a dual cchc-type classical zinc fingers
Analyse The hantavirus glycoprotein G1 tail contains a dual cchc-type classical zinc… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2K9H
- Type
- protein
- Length
- 57 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycoprotein
- UniProt
- Q99BV0
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 33% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycoprotein | protein | 57 | 33% helix, 7% strand | Q99BV0 |
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
- 2K9H · The hantavirus glycoprotein G1 tail contains a dual CCHC-type classical zinc fingers · 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 Q99BV0
- Elsewhere: RCSB PDB 2K9H · PDBe 2K9H · UniProt Q99BV0
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