Research workbench
Structural insights into de multifunctional VP3 protein of BIRNAVIRUSES:GOLD derivative
Analyse Structural insights into de multifunctional VP3 protein of BIRNAVIRUSES:GOLD… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z7J
- Type
- protein
- Length
- 125 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid assembly protein VP3
- UniProt
- P25220
- Ligands
- AU
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Capsid assembly protein VP3 | protein | 125 | 58% helix, 0% strand | P25220 |
Ligands and binding sites
- AU · Gold ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2Z7J · Structural insights into de multifunctional VP3 protein of birnaviruses:gold derivative · 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 P25220
- Elsewhere: RCSB PDB 2Z7J · PDBe 2Z7J · UniProt P25220
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