Research workbench
NMR structure calculation of a composite CYS2HIS2 type zinc finger protein containing a non-peptide (or oligourea) helical domain
Analyse NMR structure calculation of a composite CYS2HIS2 type zinc finger protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5N14
- Type
- protein
- Length
- 25 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (chimeric oligourea-peptide zinc finger)
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 20% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (chimeric oligourea-peptide zinc finger) | protein | 25 | 20% helix, 16% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 8 modified (nonstandard).
Compared structures
- 5N14 · NMR structure calculation of a composite Cys2His2 type zinc finger protein containing a… · 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
- Elsewhere: RCSB PDB 5N14 · PDBe 5N14
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