Research workbench
NMR structure of the C-terminal domain of the human RPAP3 protein
Analyse NMR structure of the C-terminal domain of the human RPAP3 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EZ4
- Type
- protein
- Length
- 135 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA polymerase II-associated protein 3
- UniProt
- Q9H6T3
Structure
solution nmr · 1 distinct chain · 66% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase II-associated protein 3 | protein | 135 | 66% helix, 0% strand | Q9H6T3 |
Compared structures
- 6EZ4 · NMR structure of the C-terminal domain of the human RPAP3 protein · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H6T3 · AlphaFold monomer V2.0 prediction for RNA polymerase II-associated protein 3 (Q9H6T3) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 Q9H6T3
- Elsewhere: RCSB PDB 6EZ4 · PDBe 6EZ4 · UniProt Q9H6T3
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