Research workbench
Crystal structure of the S. cerevisiae RTF1 histone modification domain mutant R124A R126A R128A
Analyse Crystal structure of the S. cerevisiae RTF1 histone modification domain mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EMX
- Type
- protein
- Length
- 107 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA polymerase-associated protein RTF1
- UniProt
- P53064
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase-associated protein RTF1 | protein | 53 | 66% helix, 4% strand | P53064 |
| B | RNA polymerase-associated protein RTF1 | protein | 54 | 67% helix, 4% strand | P53064 |
Compared structures
- 5EMX · Crystal structure of the S. cerevisiae Rtf1 histone modification domain mutant R124A… · the same entry in another collection · chain A against A, TM-score 1.00
- P53064 · AlphaFold monomer V2.0 prediction for RNA polymerase-associated protein RTF1 (P53064) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 P53064
- Elsewhere: RCSB PDB 5EMX · PDBe 5EMX · UniProt P53064
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