Research workbench
Structure of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy; a new structural class of zinc-finger
Analyse Structure of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy; a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CHC
- Type
- protein
- Length
- 68 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Equine herpes virus-1 ring domain
- UniProt
- P28990
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 12% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Equine herpes virus-1 ring domain | protein | 68 | 12% helix, 12% strand | P28990 |
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
- 1CHC · Structure of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy; a new… · 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 P28990
- Elsewhere: RCSB PDB 1CHC · PDBe 1CHC · UniProt P28990
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