MolNFT v1 · #22763 · protein
A novel zn finger motif in the basal transcriptional machinery: three- dimensional NMR studies of the nucleic-acid binding domain of transcriptional elongation factor tfiis
1TFI · Transcriptional elongation factor sii: “A novel zn finger motif in the basal transcriptional machinery: three- dimensional NMR studies of the…”. Solution nmr, 1 ligand (ZN). MolNFT v1 #22763 on GenesisL1: 3D structure, binding sites…
- PDB
- 1TFI
- Type
- protein
- Length
- 50 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional elongation factor sii
- UniProt
- P23193
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 0% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional elongation factor sii | protein | 50 | 0% helix, 34% strand | P23193 |
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.
Compared structures
- 1TFI · A novel zn finger motif in the basal transcriptional machinery: three-dimensional NMR… · the same entry in another collection · chain A against A, TM-score 1.00
- P23193 · AlphaFold monomer V2.0 prediction for transcription elongation factor a protein 1 (P23193) · a predicted model of the same protein · chain A against A, TM-score 0.73
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 P23193
- Elsewhere: RCSB PDB 1TFI · PDBe 1TFI · UniProt P23193
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